US2018355394A1PendingUtilityA1

Bioconversion of short-chain hydrocarbons to fuels and chemicals

Assignee: GONZALES RAMONPriority: Mar 31, 2015Filed: Mar 31, 2016Published: Dec 13, 2018
Est. expiryMar 31, 2035(~8.7 yrs left)· nominal 20-yr term from priority
Inventors:Ramon Gonzales
C12Y 102/04001C12Y 602/01005C12Y 103/99C12Y 101/01C12P 7/02C12N 9/001C12Y 402/01002C12N 9/88C12P 13/001C12Y 401/01047C12N 9/93C12N 9/0008C12Y 208/03C12Y 207/01031C12P 7/40C12Y 203/01012C12Y 114/15003C12Y 108/01004C12Y 602/01C12P 19/32C12Y 504/99C12Y 102/01C12P 5/02C12P 13/04C12Y 401/03024C12Y 401/00C12Y 504/02C12N 9/13C12Y 504/99002C12Y 402/01011C12Y 402/01C12Y 501/99002C12P 9/00C12Y 401/01C12P 7/46C12N 9/0006C12P 7/24C12N 9/90C12P 7/42C12Y 203/01054C12Y 101/03039C12N 9/0077C12P 5/026C12Y 504/99001C12Y 103/05001C12Y 501/99001C12Y 604/01003C12N 9/00C12P 7/625Y02E50/30
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Claims

Abstract

An engineered microorganism(s) with novel pathways for the conversion of short-chain hydrocarbons to fuels and chemicals (e.g. carboxylic acids, alcohols, hydrocarbons, and their alpha-, beta-, and omega-functionalized derivatives) is described. Key to this approach is the use of hydrocarbon activation enzymes able to overcome the high stability and low reactivity of hydrocarbon compounds through the cleavage of an inert C—H bond. Oxygen-dependent or oxygen-independent activation enzymes can be exploited for this purpose, which when combined with appropriate pathways for the conversion of activated hydrocarbons to key metabolic intermediates, enables the generation of product precursors that can subsequently be converted to desired compounds through established pathways. These novel engineered microorganism(s) provide a route for the production of fuels and chemicals from short chain hydrocarbons such as methane, ethane, propane, butane, and pentane.

Claims

exact text as granted — not AI-modified
We claim: 
     
         1 . A genetically engineered microorganism with one or more expression vectors or integrated sequences encoding overexpressed 1) alkane monooxygenase or alkane hydroxylase (EC 1.14.15.3), 2) alcohol dehydrogenase (EC 1.1.1.-), 3) aldehyde dehydrogenase (EC 1.2.1.-), and 4) acyl-CoA synthetase (EC 6.2.1.-); wherein said microorganism is able to convert a short chain alkane (C1-C5) to an acyl-CoA. 
     
     
         2 . A genetically engineered microorganism with one or more expression vectors or integrated sequences encoding overexpressed 1) alkyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-alkyl-malonyl-CoA mutase (EC 5.4.99.-), 4) 2-methyl-alkyl-malonyl-CoA decarboxylase (EC 4.1.1.-), 5) propionyl-CoA carboxylase (EC 6.4.1.3), 6) methylmalonyl-CoA epimerase (EC 5.1.99.1), 7) methylmalonyl-CoA mutase (EC 5.1.99.2), 8) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or succinyl-CoA synthetase (EC 6.2.1.5), and 9) succinate dehydrogenase (EC 1.3.5.1), wherein said microorganism is able to convert a short chain alkane (C1-C5) to an acyl-CoA through fumarate addition to said short chain alkane and subsequent regeneration of said fumarate. 
     
     
         3 . A genetically engineered microorganism with one or more expression vectors or integrated sequences encoding overexpressed 1) methyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-succinyl-CoA dehydrogenase (EC 1.3.99.-), 4) mesaconyl-C1-CoA-C4-CoA transferase (EC 2.8.3.-), 5) mesaconyl-C4-CoA hydratase (EC 4.2.1.153), 6) L-malyl-CoA/citramalyl-CoA lyase (EC 4.1.3.25), 7) pyruvic-malic carboxylase (EC 1.1.1.39), and 8) fumarase (EC 4.2.1.2), wherein said microorganism is able to convert methane to an acyl-coA through fumarate addition to said methane and subsequent regeneration of said fumarate. 
     
     
         4 . A genetically engineered microorganism with one or more expression vectors encoding overexpressed 1) methyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-alkyl-succinyl-CoA dehydrogenase (EC 1.3.99.-), 4) mesaconyl-CoA hydratase/β-methylmalyl-CoA dehydratase (EC 4.2.1.148), 5) β-methylmalyl-CoA lyase (EC 4.1 3.24), 6) propionyl-CoA carboxylase (EC 6.4.1.3), 7) methylmalonyl-CoA epimerase (EC 5.1.99.1) and methylmalonyl-CoA mutase (EC 5.1.99.2), 8) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or succinyl-CoA synthetase (EC 6.2.1.5), 9) succinate dehydrogenase (EC 1.3.5.1), 10: glyoxylate carboligase (EC 4.1.1.47), 11) tartronate semialdehyde reductase (EC 1.1.1.60), 12) glycerate kinase (EC 2.7.1.31), 13:) glycolytic enzymes (phosphoglycerate mutase (EC 5.4.2.11), enolase (EC 4.2.1.11), pyruvate kinase (EC 2.7.1.40)), and 14) pyruvate dehydrogenase complex (EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4) or pyruvate formate lyase (EC 2.3.1.54), wherein said microorganism is able to convert methane to an acyl-coA through fumarate addition to said methane and subsequent regeneration of said fumarate. 
     
     
         5 . A genetically engineered microorganism being  E. coli  and comprising one or more expression vectors or integrated sequences encoding overexpressed 1) alkane monooxygenase or alkane hydroxylase (EC 1.14.15.3), 2) alcohol dehydrogenase (EC 1.1.1.-), 3) aldehyde dehydrogenase (EC 1.2.1.-), and 4) acyl-CoA synthetase (EC 6.2.1.-); wherein said microorganism is able to convert a short chain alkane (C1-C5) to an acyl-CoA. 
     
     
         6 . A genetically engineered microorganism being  E. coli  and comprising one or more expression vectors or integrated sequences encoding overexpressed 1) alkyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-alkyl-malonyl-CoA mutase (EC 5.4.99.-), 4) 2-methyl-alkyl-malonyl-CoA decarboxylase (EC 4.1.1.-), 5) propionyl-CoA carboxylase (EC 6.4.1.3), 6) methylmalonyl-CoA epimerase (EC 5.1.99.1), 7) methylmalonyl-CoA mutase (EC 5.1.99.2), 8) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or succinyl-CoA synthetase (EC 6.2.1.5), and 9) succinate dehydrogenase (EC 1.3.5.1), wherein said microorganism is able to converts a short chain alkane (C1-C5) to an acyl-CoA through fumarate addition to said short chain alkane and subsequent regeneration of said fumarate. 
     
     
         7 . A genetically engineered microorganism being  E. coli  and comprising one or more expression vectors or integrated sequences encoding overexpressed 1) methyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-succinyl-CoA dehydrogenase (EC 1.3.99.-), 4) mesaconyl-C1-CoA-C4-CoA transferase (EC 2.8.3.), 5) mesaconyl-C4-CoA hydratase (EC 4.2.1.153), 6) L-malyl-CoA/citramalyl-CoA lyase (EC 4.1.3.25), 7) pyruvic-malic carboxylase (EC 1.1.1.39), and 8) fumarase (EC 4.2.1.2), wherein said microorganism is able to convert methane to an acyl-coA through fumarate addition to said methane and subsequent regeneration of said fumarate. 
     
     
         8 . A genetically engineered microorganism being  E. coli  and comprising one or more expression vectors or integrated sequences encoding overexpressed 1) methyl succinate synthase (EC 4.1.-), 2) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or 2-methyl-alkyl-succinyl-CoA synthetase (EC 6.2.1.-), 3) 2-methyl-alkyl-succinyl-CoA dehydrogenase (EC 1.3.99.-), 4) mesaconyl-CoA hydratase/β-methylmalyl-CoA dehydratase (EC 4.2.1.148), 5) β-methylmalyl-CoA lyase (EC 4.1.3.24), 6) propionyl-CoA carboxylase (EC 6.4.1.3), 7) methylmalonyl-CoA epimerase (EC 5.1.99.1) and methylmalonyl-CoA mutase (EC 5.1.99.2), 8) succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase (EC 2.8.3.-) or succinyl-CoA synthetase (EC 6.2.1.5), 9) succinate dehydrogenase (EC 1.3.5.1), 10: glyoxylate carboligase (EC 4.1.1.47), 11) tartronate semialdehyde reductase (EC 1.1.1.60), 12) glycerate kinase (EC 2.7.1.31), 13:) glycolytic enzymes (phosphoglycerate mutase (EC 5.4.2.11), enolase (EC 4.2.1.11), pyruvate kinase (EC 2.7.1.40)), and 14) pyruvate dehydrogenase complex (EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4) or pyruvate formate lyase (EC 2.3.1.54), wherein said microorganism is able to convert methane to an acyl-coA through fumarate addition to said methane and subsequent regeneration of said fumarate. 
     
     
         9 . The genetically engineered microorganism of  claims 1 - 8  wherein said expression vectors are inducible expression vectors or said integrated sequences are inducible integrated sequences. 
     
     
         10 . A genetically engineered microorganism converting a short-chain (C1-C5) alkane substrate to a product, said microorganism comprising enzymes or overexpressed enzymes catalyzing:
 a) a sequence of reactions a pathway for the oxygen-independent activation of a short-chain (C1-C5) alkane via fumarate addition to a 2-methyl-alkyl-succinate and subsequent conversion of said 2-methyl-alkyl-succinate to an acyl-CoA;   b) a sequence of reactions of a pathway for the generation of product precursor acetyl-CoA and an acyl-CoA or keto-acid from said acyl-CoA;   c) a sequence of reactions of a pathway for the regeneration of fumarate from said acyl-CoA or keto-acid to fumarate through conversion;   d) a sequence of reactions of a pathway for the formation of a desired product from said acetyl-CoA intermediate.   
     
     
         11 . A genetically engineered microorganism converting a short-chain (C1-C5) alkane substrate to a product, said microorganism comprising enzymes or overexpressed enzymes catalyzing:
 a) a sequence of reactions of a pathway for the oxygen-dependent activation of a short-chain (C1-C5) alkane to a primary alcohol via terminal addition of a hydroxyl group and subsequent conversion of said alcohol to an acyl-CoA;   b) a sequence of reactions for the generation of product precursor acetyl-CoA from said acyl-CoA; and   c) a sequence of reactions of a pathway for the formation of a desired product from said acetyl-CoA intermediate.   
     
     
         12 . The microorganism of  claim 10 , wherein said pathway for the oxygen-independent activation and conversion to an acyl-CoA comprises:
 a) an overexpressed alkyl succinate synthase that catalyzes the addition of fumarate to a short-chain (C1-C5) alkane to produce a 2-methyl-alkyl-succinate;   b) an overexpressed succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase or 2-methyl-alkyl-succinyl-CoA synthetase that catalyzes the conversion of said 2-methyl-alkyl-succinate to a 2-methyl-alkyl-succinyl-CoA;   c) an overexpressed 2-methyl-alkyl-malonyl-CoA mutase that catalyzes the isomerization of said 2-methyl-alkyl-succinyl-CoA to a 2-methyl-alkyl-malonyl-CoA; and   d) an overexpressed 2-methyl-alkyl-malonyl-CoA decarboxylase that catalyzes the decarboxylation of said 2-methyl-alkyl-malonyl-CoA to an acyl-CoA.   
     
     
         13 . The microorganism of  claim 10 , wherein said pathways for the oxygen-independent activation and conversion to an acyl-CoA and generation of product precursor acetyl-CoA and an acyl-CoA or keto-acid comprises:
 a) an overexpressed alkyl succinate synthase that catalyzes the addition of fumarate to a short-chain (C1-C5) alkane to produce a 2-methyl-alkyl-succinate;   b) an overexpressed 2-methyl-alkyl-succinyl-CoA synthetase that catalyzes the conversion of said 2-methyl-alkyl-succinate to a 2-methyl-alkyl-succinyl-CoA;   c) an overexpressed 2-methyl-alkyl-succinyl-CoA dehydrogenase that catalyzes the conversion of said 2-methyl-alkyl-succinyl-CoA to 2-methyl-alkyl-2-butenoyl-CoA;   d) an overexpressed mesaconyl-C1-CoA-C4-CoA transferase that catalyzes the conversion of said 2-methyl-alkyl-2-butenoyl-CoA to 3-methyl-alkyl-2-butenoyl-CoA;   e) an overexpressed mesaconyl-C4-CoA hydratase that catalyzes the conversion of said 3-methyl-alkyl-2-butenoyl-CoA to 3-methyl-alkyl-3-hydroxy-succinyl-CoA; and   f) an overexpressed citramalyl-CoA lyase that catalyzes the conversion of said 3-methyl-alkyl-3-hydroxy-succinyl-CoA to acetyl-CoA and a keto-acid.   
     
     
         14 . The microorganism of  claim 10 , wherein said pathways for the oxygen-independent activation and conversion to an acyl-CoA and generation of product precursor acetyl-CoA and an acyl-CoA or keto-acid comprises:
 a) an overexpressed alkyl succinate synthase that catalyzes the addition of fumarate to a short-chain (C1-C5) alkane to produce a 2-methyl-alkyl-succinate;   b) an overexpressed succinyl-CoA2-methyl-alkyl-succinyl-CoA transferase or 2-methyl-alkyl-succinyl-CoA synthetase that catalyzes the conversion of said 2-methyl-alkyl-succinate to a 2-methyl-alkyl-succinyl-CoA;   c) an overexpressed 2-methyl-alkyl-succinyl-CoA dehydrogenase that catalyzes the conversion of said 2-methyl-alkyl-succinyl-CoA to 2-methyl-alkyl-2-butenoyl-CoA;   d) an overexpressed mesaconyl-CoA hydratase/β-methylmalyl-CoA dehydratase that catalyzes the conversion of said 2-methyl-alkyl-2-butenoyl-CoA to 3-hydroxy-2-methyl-alkyl-succinyl-CoA;   e) an overexpressed 3-methylmalyl-CoA lyase that catalyzes the conversion of said 3-hydroxy-2-methyl-alkyl-succinyl-CoA to glyoxylate and an acyl-CoA;   f) an overexpressed glyoxylate carboligase that catalyzes the conversion of said glyoxylate to tartronate semialdehyde;   g) an overexpressed tartronate semialdehyde reductase that catalyzes the conversion of said tartronate semialdehyde to D-glycerate;   h) an overexpressed glycerate kinase that catalyzes the conversion of said D-glycerate to 3-phospho-D-glycerate;   i) glycolytic enzymes (phosphoglycerate mutase, enolase, pyruvate kinase) that catalyze the conversion of said 3-phospho-D-glycerate to pyruvate; and   j) a pyruvate formate lyase or pyruvate dehydrogenase that catalyze the conversion of said pyruvate to acetyl-CoA.   
     
     
         15 . The microorganism of  claim 12 , wherein said pathway for the generation of product precursor acetyl-CoA and an acyl-CoA or keto-acid comprises:
 a) an overexpressed acyl-CoA dehydrogenase that catalyzes the conversion of said acyl-CoA to a transenoyl-CoA;   b) an overexpressed enoyl-CoA hydratase that catalyzes the hydration of said transenoyl-CoA to a 3-hydroxyacyl-CoA;   c) an overexpressed 3-hydroxyacyl-CoA dehydrogenase that catalyzes the oxidation of said 3-hydroxyacyl-CoA to a β-ketoacyl-CoA; and   d) an overexpressed thiolase that catalyzes the cleavage of an acetyl-CoA from said β-ketoacyl-CoA to produce acetyl-CoA and an acyl-CoA 2-carbons shorter than said starting acyl-CoA.   
     
     
         16 . The microorganism of  claim 12  or  14 , wherein said pathway for the regeneration of fumarate from an acyl-CoA or keto-acid comprises:
 a) an overexpressed propionyl-CoA carboxylase that catalyzes the carboxylation of propionyl-CoA to (S)-methyl-malonyl-CoA; 
 b) an overexpressed methyl-malonyl-CoA epimerase that catalyzes the interconversion of said (S)-methyl-malonyl-CoA to (R)-methyl-malonyl-CoA; 
 c) an overexpressed methyl-malonyl-CoA mutase that catalyzes the isomerization of said (R)-methyl-malonyl-CoA to succinyl-CoA; and 
 d) an overexpressed succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase or succinyl-CoA synthetase that catalyzes the conversion of said succinyl-CoA to succinate. 
 
     
     
         17 . The microorganism of  claim 13 , wherein said pathway for the regeneration of fumarate from an acyl-CoA or keto-acid comprises:
 a) an overexpressed malate dehydrogenase for the conversion of said keto-acid (pyruvate) to malate; and   b) an overexpressed fumarase for the dehydration of malate to fumarate.   
     
     
         18 . The microorganism of  claim 13 , wherein said pathway for the regeneration of fumarate from an acyl-CoA or keto-acid comprises:
 a) an overexpressed carboxylic acid omega hydroxylase that catalyzes the conversion of said keto-acid to an omega-hydroxy-2-keto-acid;   b) an overexpressed alcohol dehydrogenase that catalyzes the conversion of said omega-hydroxyketo-acid to an omega-oxo-2-keto-acid;   c) an overexpressed aldehyde dehydrogenase that catalyzes the conversion of said omega-oxo-keto-acid to a dicarboxylic 2-keto-acid;   d) an overexpressed ketoreductase or malate dehydrogenase that catalyzes the conversion of said dicarboxylic 2-keto-acid to malate; and   e) an overexpressed fumarase for the dehydration of malate to fumarate.   
     
     
         19 . The microorganism of  claim 11 , wherein said pathway for the oxygen-dependent activation and conversion to an acyl-CoA comprises:
 a) an overexpressed alkane monooxygenase or alkane hydroxylase that catalyzes the terminal hydroxylation of a short-chain (C1-C5) alkane to produce a primary alcohol;   b) an overexpressed alcohol dehydrogenase that catalyzes the oxidation of said primary alcohol to produce an aldehyde;   c) an overexpressed aldehyde dehydrogenase that catalyzes the oxidation of said aldehyde to produce a carboxylic acid and an overexpressed acyl-CoA synthetase that catalyzes the conversion of said carboxylic acid to an acyl-CoA, or an overexpressed acylating aldehyde dehydrogenase that catalyzes the conversion of said aldehyde to an acyl-CoA.   
     
     
         20 . The microorganism of  claim 12 , wherein said pathway for the generation of product precursor acetyl-CoA comprises:
 a) an overexpressed acyl-CoA dehydrogenase that catalyzes the conversion of said acyl-CoA to a transenoyl-CoA;   b) an overexpressed enoyl-CoA hydratase that catalyzes the hydration of said transenoyl-CoA to a 3-hydroxyacyl-CoA;   c) an overexpressed 3-hydroxyacyl-CoA dehydrogenase that catalyzes the oxidation of said 3-hydroxyacyl-CoA to a β-ketoacyl-CoA;   d) an overexpressed thiolase that catalyzes the cleavage of an acetyl-CoA from said β-ketoacyl-CoA to produce acetyl-CoA and an acyl-CoA 2-carbons shorter than said starting acyl-CoA.   
     
     
         21 . The microorganism of  claim 10  or  11 , wherein said pathway for the formation of a desired product from said acetyl-CoA intermediate is a reverse beta oxidation (BOX-R) cycle that grows a primer by adding a 2-carbon donor thereto in each cycle, said BOX-R cycle comprising:
 a) an overexpressed thiolase that catalyzes the non-decarboxylative condensation of an acyl-CoA primer with a 2-carbon donor acetyl-CoA to produce a β-ketoacyl-CoA; 
 b) an overexpressed 3-oxoacyl-[acyl-carrier-protein] reductase or overexpressed 3-hydroxyacyl-CoA dehydrogenase that catalyzes the reduction of a β-ketoacyl-CoA to a β-hydroxyacyl-CoA; 
 c) an overexpressed 3-hydroxyacyl-[acyl-carrier-protein] dehydratase or an overexpressed enoyl-CoA hydratase or 3-hydroxyacyl-CoA dehydratase that catalyzes the dehydration of a (3R)-β-hydroxyacyl-CoA to a transenoyl-CoA; 
 d) an overexpressed enoyl-[acyl-carrier-protein] reductase or acyl-CoA dehydrogenase or trans-enoyl-CoA reductase that catalyzes the reduction of a transenoyl-CoA to an acyl-CoA that is two carbons longer than said acyl-CoA primer; and 
 e) an overexpressed termination pathway that catalyzes the exit of an intermediate from said BOX-R cycle. 
 
     
     
         22 . The microorganism of  claim 10  or  11 , wherein said pathway for the formation of a desired product from said acetyl-CoA intermediate is a the fatty acid biosynthesis (FAS) pathway that grows a primer by adding a 2-carbon donor thereto in each cycle, said FAS pathway comprising:
 a) an overexpressed acetyl-CoA carboxylase that catalyzes the conversion of acetyl-CoA to malonyl-CoA; 
 b) an overexpressed malonyl-CoA-[acyl-carrier-protein] (“ACP”) transacylase that catalyzes the conversion of said malonyl-CoA to malonyl-ACP; 
 c) an overexpressed 3-ketoacyl-ACP synthase that catalyzes the decarboxylative condensation of said malonyl-ACP with an acyl-ACP primer to produce a β-ketoacyl-ACP; 
 d) an overexpressed 3-oxoacyl-ACP reductase that catalyzes the reduction of a β-ketoacyl-ACP to a β-hydroxyacyl-ACP; 
 e) an overexpressed 3-hydroxyacyl-ACP dehydratase that catalyzes the dehydration of a (3R)-β-hydroxyacyl-ACP to a transenoyl-ACP; 
 f) an overexpressed enoyl-ACP reductase that catalyzes the reduction of a transenoyl-ACP to an acyl-ACP that is two carbons longer than said acyl-ACP primer; and 
 g) an overexpressed termination pathway that catalyzes the exit of an intermediate from said FAS cycle. 
 
     
     
         23 . The microorganism of  claim 21 , wherein said termination pathway is selected from the group consisting of i) a CoA cleaving thioesterase, ii) an acyl-CoA:acetyl-CoA transferase, and iii) a phosphotransacylase and a carboxylate kinase. 
     
     
         24 . The microorganism of  claim 22 , wherein said termination pathway is an ACP cleaving thioesterase. 
     
     
         25 . The microorganism of  claim 23  or  24 , wherein said microorganism produces a product selected from the group consisting of carboxylic acids, (3R)-β-hydroxy carboxylic acids, β-keto carboxylic acids, and α,β-unsaturated carboxylic acids. 
     
     
         26 . The microorganism of  claim 21 , wherein said termination pathway is selected from the group consisting of i) an alcohol-forming coenzyme-A thioester reductase, and ii) an aldehyde-forming CoA thioester reductase and an alcohol dehydrogenase. 
     
     
         27 . The microorganism of  claim 21 , wherein said termination pathway is selected from the group consisting of i) an alcohol-forming ACP thioester reductase, and ii) an aldehyde-forming ACP thioester reductase and an alcohol dehydrogenase. 
     
     
         28 . The microorganism of  claim 26  or  27 , wherein said microorganism produces a product selected from the group consisting of primary alcohols, 1,(3R)-β diols, β-keto primary alcohols, and α,β-unsaturated primary alcohols. 
     
     
         29 . The microorganism of  claim 21 , wherein said termination pathway consists of an aldehyde-forming CoA thioester reductase and an aldehyde decarbonylase. 
     
     
         30 . The microorganism of  claim 22 , wherein said termination pathway consists of an aldehyde-forming ACP thioester reductase and an aldehyde decarbonylase. 
     
     
         31 . The microorganism of  claim 29  or  30 , wherein said microorganism produces a product selected from the group consisting of linear alkanes, linear alkan-2-ols, linear methyl-ketones, and 1-alkenes. 
     
     
         32 . The microorganism of  claim 21 , wherein said termination pathway consists of an aldehyde-forming CoA thioester reductase and a transaminase. 
     
     
         33 . The microorganism of  claim 22 , wherein said termination pathway consists of an aldehyde-forming ACP thioester reductase and a transaminase. 
     
     
         34 . The microorganism of  claim 32  or  33 , wherein said microorganism produces a product selected from the group consisting of primary amines, 3-hydroxy-amines, 3-keto-amines, and α,β-unsaturated primary amines. 
     
     
         35 . The microorganism of  claim 25 , wherein said microorganism expresses a carboxylic acid omega hydroxylase and produces a product selected from the group consisting of w-hydroxylated carboxylic acids, (3R)-β-, ω-dihydroxy carboxylic acids, β-keto, co-hydroxy carboxylic acids, and α,β-unsaturated ω-hydroxylated carboxylic acids. 
     
     
         36 . The microorganism of  claim 28 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, an alcohol oxidase, and an aldehyde dehydrogenase, and produces a product selected from the group consisting of ω-hydroxylated carboxylic acids, (3R)-β-, ω-dihydroxy carboxylic acids, β-keto, ω-hydroxy carboxylic acids, and α,β-unsaturated omega-hydroxylated carboxylic acids. 
     
     
         37 . The microorganism of  claim 28 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, and produces a product selected from the group consisting of 1-,ω-diols, 1-,(3R)-β-, ω-triols, β-keto, 1-,ω-diols, and α,β-unsaturated 1-,ω-diols. 
     
     
         38 . The microorganism of  claim 25 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, an alcohol oxidase, and an aldehyde dehydrogenase, and produces a product selected from the group consisting of di-carboxylic acids, (3R)-β-hydroxy di-carboxylic acids, β-keto di-carboxylic acids, and α,β-unsaturated di-carboxylic acids. 
     
     
         39 . The microorganism of  claim 28 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, an alcohol oxidase, and a transaminase, and produces a product selected from the group consisting of primary alkanolamines (i.e. 1, ω-hydroxyamines), (3R)-β-hydroxy primary alkanolamines, β-keto primary alkanolamines, and α,β-unsaturated primary alkanolamines. 
     
     
         40 . The microorganism of  claim 34 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, and produces a product selected from the group consisting of primary alkanolamines (i.e. 1, ω-hydroxyamines), (3R)-β-hydroxy primary alkanolamines, β-keto primary alkanolamines, and α,β-unsaturated primary alkanolamines. 
     
     
         41 . The microorganism of  claim 34 , wherein said microorganism expresses a carboxylic acid ω hydroxylase, an alcohol oxidase, and an aldehyde dehydrogenase, and produces a product selected from the group consisting of ω-amino acids, (3R)-β-hydroxy ω-amino acids, 3-keto ω-amino acids, and α,β-unsaturated ω-amino acids. 
     
     
         42 . The microorganism of  claim 25 , wherein said microorganism expresses a carboxylic acid alpha hydroxylase, and produces a product selected from the group alpha-hydroxy carboxylic acids, alpha-, (3R)-β-dihydroxy carboxylic acids, α-hydroxy, β-keto carboxylic acids, and α,β-unsaturated α-hydroxy carboxylic acids. 
     
     
         43 . The microorganism of  claim 28 , wherein said microorganism expresses a carboxylic acid α hydroxylase, and produces a product selected from the group consisting of 1,2-diols, 1,2,3-triols, β-keto, 1,2-diols, and α,β-unsaturated 1,2-diols. 
     
     
         44 . The microorganism of  claim 34 , wherein said microorganism expresses a carboxylic acid α hydroxylase, and produces a product selected from the group consisting of α-hydroxylated primary amines, α-, β-dihydroxy primary amines, α-hydroxy, β-keto primary amines, and α-hydroxy, α,β-unsaturated primary amines. 
     
     
         45 . The microorganisms of  claim 10  or  11 , further comprising reduced expression of fermentation enzymes leading to reduced production of lactate, acetate, ethanol and succinate. 
     
     
         46 . The microorganism of  claim 12 ,  13 , or  14 , wherein said overexpressed alkyl succinate synthase is encoded by  Azoarcus  sp. HxN1 masBCDEG (A9J4K0, A9J4K2, A9J4K4, A9J4K6, A9J4J6),  Desulfatibacillum alkenivorans  assA1/FassB1/assC1/assD1 (ACL03428.1, ACL03427.1, ACL03427.1, ACL03425.1),  Desulfosarcina  sp. BuS5 A39W_RS0101550/A39W_RS0101545/A39W RS0101540/A39W_RS0101535/A39W_RS19630/A39W_RS0101580 (WP_027352796.1, WP_027352795.1, WP_027352794.1, WP_027352793.1, WP_051374532.1, WP_027352800.1),  Desulfatibacillum alkenivorans  assA2/assB2/assC2/assD2 (ACL03892.1, ACL03893.1, ACL03891.1, ACL03895.1),  Peptococcaceae  sp. SCADC (WP_036747468.1),  Aromatoleum  sp. OcN1 masD (CBK27727.1),  Desulfoglaeba alkanexedens  assA (ADJ51097.1), or homologues thereof. 
     
     
         47 . The microorganism of  claim 12  or  14 , wherein said overexpressed succinyl-CoA:2-methyl-alkyl-succinyl-CoA transferase or 2-methyl-alkyl-succinyl-CoA synthetase is encoded by  Chloroflexus aurantiacus  sct (A9WGE3),  Thauera aromatica  bbsEF (Q9KJF0, Q9KJE9),  Escherichia coli  sucCD (P0A836, P0AGE9),  Desulfatibacillum alkenivorans  Dalk_1737 (B8FFM9), or homologues thereof. 
     
     
         48 . The microorganism of  claim 12 , wherein said overexpressed 2-methyl-alkyl-malonyl-CoA mutase is encoded by  Desulfatibacillum alkenivorans  Dalk_0220/Dalk_0221 (ACL01930.1, ACL01929.1), or homologues. 
     
     
         49 . The microorganism of  claim 12 , wherein said overexpressed 2-methyl-alkyl-malonyl-CoA decarboxylase is encoded by  Desulfatibacillum alkenivorans  Dalk_1740 (B8FFN2), or homologues thereof. 
     
     
         50 . The microorganism of  claim 13  or  14 , wherein said overexpressed 2-methyl-alkyl-succinyl-CoA dehydrogenase is encoded by  Rhodobacter sphaeroides  mcd (ADC44452.1) or homologues thereof. 
     
     
         51 . The microorganism of  claim 13 , wherein said overexpressed mesaconyl-C1-CoA-C4-CoA transferase is encoded by  Chloroflexus aurantiacus  mct (A9WC36) or homologues thereof. 
     
     
         52 . The microorganism of  claim 13 , wherein said overexpressed mesaconyl-C4-CoA hydratase is encoded by  Chloroflexus aurantiacus  meh (A9WC41) or homologues thereof. 
     
     
         53 . The microorganism of  claim 13 , wherein said overexpressed citramalyl-CoA lyase is encoded by  Chloroflexus aurantiacus  mclA (A9WC35) or homologues thereof. 
     
     
         54 . The microorganism of  claim 14 , wherein said overexpressed mesaconyl-CoA hydratase/β-methylmalyl-CoA dehydratase is encoded by  Chloroflexus aurantiacus  mch (A9WC34),  Rhodobacter sphaeroides  mch (Q31Z78), or homologues thereof. 
     
     
         55 . The microorganism of  claim 14 , wherein said overexpressed β-methylmalyl-CoA lyase is encoded by  Rhodobacter sphaeroides  mclI (B9KLE8) or homologues thereof. 
     
     
         56 . The microorganism of  claim 14 , wherein said overexpressed glyoxylate carboligase is encoded by  Escherichia coli  gcl (P0AEP7), or homologues thereof. 
     
     
         57 . The microorganism of  claim 14 , wherein said overexpressed tartronate semialdehyde reductase is encoded by  Escherichia coli  glxR (P77161), or homologues thereof. 
     
     
         58 . The microorganism of  claim 14 , wherein said overexpressed glycerate kinase is encoded by  Escherichia coli  glxK (P77364), or homologues thereof. 
     
     
         59 . The microorganism of  claim 14 , wherein said overexpressed glycerate kinase is encoded by  Escherichia coli  glxK (P77364), or homologues thereof. 
     
     
         60 . The microorganism of  claim 14 , wherein said phosphoglycerate mutase is encoded by  Escherichia coli  gpmA (P62707),  Escherichia coli  gpmM (P37689), or homologues thereof. 
     
     
         61 . The microorganism of  claim 14 , wherein said enolase is encoded by  Escherichia coli  eno (P0A6P9), or homologues thereof. 
     
     
         62 . The microorganism of  claim 14 , wherein said pyruvate kinase is encoded by  Escherichia coli  pykA (P21599),  Escherichia coli  pykF (POAD61), or homologues thereof. 
     
     
         63 . The microorganism of  claim 14 , wherein said pyruvate formate lyase is encoded by  Escherichia coli  pfiB/pflA (P09373) or homologues thereof. 
     
     
         64 . The microorganism of  claim 14 , wherein said pyruvate dehydrogenase is encoded by  Escherichia coli  aceEF/lpd (P0AFG8, P06959, C3TQA2) or homologues. 
     
     
         65 . The microorganism of  claim 14 , wherein said overexpressed acyl-CoA dehydrogenase is encoded by  Ascaris suum  ACDH (Q08523),  Escherichia coli  fadE (AP 000876.1), or homologues thereof. 
     
     
         66 . The microorganism of  claim 15 , wherein said overexpressed enoyl-CoA hydratase encoded by  Pseudomonas putida  fadBlx (NP 744366.1),  Pseudomonas putida  phaL (NP_745413.1),  Alcanivorax borkumensis  ech1 (YP_691868.1),  Alcanivorax borkumensis  ech2 (YP_692707.1)  Alcanivorax borkumensis  phaB (YP_692246.1),  Escherichia coli  fadB (NP_418288.1), or homologues thereof. 
     
     
         67 . The microorganism of  claim 15 , wherein said overexpressed 3-hydroxyacyl-CoA dehydrogenase is encoded by  Pseudomonas putida  fadB2x (Q88KS5),  Ascaris suum  GS 18673,  Escherichia coli  fadB (NP_418288.1), or homologues thereof. 
     
     
         68 . The microorganism of  claim 15 , wherein said overexpressed thiolase is encoded by  Pseudomonas putida  fadAx (NP_744364.1),  Alcanivorax borkumensis  fadAx (YP_692368.1),  Escherichia coli  atoB (NP_416728.1),  Escherichia coli  yqeF (NP_417321.2),  Escherichia coli  fadA (YP_026272.1),  Escherichia coli  fadI (NP_416844.1),  Ralstonia eutropha  bklB (AAC38322.1), or homologues thereof. 
     
     
         69 . The microorganism of  claim 16 , wherein said overexpressed propionyl-CoA carboxylase is encoded by  Chloroflexus aurantiacus  Caur_2034/Caur_3435 (A9WEI4, A9WKJ2),  Rhodobacter sphaeroides  pccAB (Q3J4D9, Q3J4E3), or homologues thereof. 
     
     
         70 . The microorganism of  claim 16 , wherein said overexpressed methyl-malonyl-CoA epimerase is encoded by  Metallosphaera sedula  Msed_0639 (A4YEG2) or homologues thereof. 
     
     
         71 . The microorganism of  claim 16 , wherein said overexpressed methyl-malonyl-CoA mutase is encoded by  Rhodobacter sphaeroides  mcmA (Q3J4D7), or homologues thereof. 
     
     
         72 . The microorganism of  claim 16 , wherein said overexpressed succinyl-CoA synthetase is encoded by  Escherichia coli  sucCD (P0A836, P0AGE9), or homologues thereof. 
     
     
         73 . The microorganism of  claim 17 , wherein said overexpressed malate dehydrogenase is encoded by  Escherichia coli  maeA (P26616),  Escherichia coli  maeB (P76558), or homologues thereof. 
     
     
         74 . The microorganism of  claim 17  or  18 , wherein said overexpressed fumarase is encoded by  Escherichia coli  fumA (POAC33),  Escherichia coli  fumB (P14407),  Escherichia coli  fumC (P05042), or homologues thereof. 
     
     
         75 . The microorganism of  claim 18 , wherein said overexpressed carboxylic acid omega hydroxylase is encoded by  Pseudomonas putida  alkBGT (YP_009076004.1, Q9WWW4.1, Q9L4M8.1),  Marinobacter aquaeolei  CYP153A (ABM17701.1),  Mycobacterium marinum  CYP153A16 (YP_001851443.1),  Polaromonas  sp. CYP153A (YP_548418.1),  Nicotiana tabacum  CYP94A5 (AAL54887.1),  Vicia sativa  CYP94A1 (AAD10204.1),  Vicia sativa  CYP94A2 (AAG33645.1),  Arabidopsis thaliana  CYP94B1 (BAB08810.1),  Arabidopsis thaliana  CYP86A8 (CAC67445.1),  Candida tropicalis  CYP52A1 (AAA63568.1, AAA34354.1, AAA34334.1),  Candida tropicalis  CYP_52A2 (AAA34353.2, CAA35593.1),  Homo sapiens  CYP4A11 (AAQ56847.1), or homologs thereof. 
     
     
         76 . The microorganism of  claim 18 , wherein said overexpressed alcohol dehydrogenase is encoded by  Rhodococcus ruber  SC1 cddC (AAL14237.1),  Acinetobacter  sp. SE19 chnD (AAG10028.1),  Escherichia coli  betA (NP_414845.1),  Escherichia coli  dkgA (NP_417485.4),  Escherichia coli  eutG (NP_416948.4),  Escherichia coli  fucO (NP_417279.2),  Escherichia coli  ucpA (NP_416921.4),  Escherichia coli  yahK (NP_414859.1),  Escherichia coli  ybbO (NP_415026.1),  Escherichia coli  ybdH (NP_415132.1),  Escherichia coli  yiaY (YP_026233.1),  Escherichia coli  yjgB (NP_418690.4), or homologues thereof. 
     
     
         77 . The microorganism of  claim 18 , wherein said overexpressed aldehyde dehydrogenase is encoded by  Rhodococcus ruber  SC1 cddD (AAL14238.1),  Acinetobacter  sp. SE19 chnE (AAG10022.1), or homologues thereof. 
     
     
         78 . The microorganism of  claim 18 , wherein said overexpressed ketoreductase/malate dehydrogenase is encoded by  Escherichia coli  mdh (P61889), or homologues thereof. 
     
     
         79 . The microorganism of  claim 19 , wherein said overexpressed alkane monooxygenase or alkane hydroxylase is encoded by  Pseudomonas putida  alkBGT (YP_009076004.1, Q9WWW4.1, Q9L4M8.1),  Mycobacterium  sp. strain HXN-1500 CYP153A6 (Q5K1Y6),  Gordonia  sp. TY-5 prmABCD (AB112920.1),  Thauera butanivorans  bmoXYZ/bmoC/bmoB (Q8KQF0, Q8KQE9, Q8KQE7, Q8KQE6, Q8KQE8),  Alcanivorax borkumensis  alkB1 (Q0VKZ3.1),  Alcanivorax borkumensis  alkB2 (QOVTH3.1),  Sphingopyxis macrogoltabida  ahpG3 (Q5F4D3),  Methylosinus trichosporium  OB3b mmoXYZBC/orfY (P27353, P27354, P27355, Q53563, P27356, Q53562),  Methylococcus capsulatus  Bath mmoXYZBC/orfY (P22869, P18798, P11987, P18797, 22868, P22867),  Rhodobacter sphaeroides  RSP2792/RSP2793/RSP2794/RSP2795 (YP_352924.1, (YP_352923.1, YP_352922.1, YP_352921.1), or homologues thereof. 
     
     
         80 . The microorganism of  claim 19 , wherein said overexpressed alcohol dehydrogenase is encoded by  Pseudomonas putida  (Q9WWW2),  Gordonia  sp. TY-5 adhI (AB112920.1),  Bacillus methanolicus  mdh (P31005),  Mycobacterium  sp. DSM 3803 mdo (C5MRT8),  Methylobacterium extorquens  moxI, moxF (P14775, P16027),  Escherichia coli  betA (NP_414845.1),  Escherichia coli  dkgA (NP_417485.4),  Escherichia coli  eutG (NP_416948.4),  Escherichia coli  fucO (NP_417279.2),  Escherichia coli  ucpA (NP_416921.4),  Escherichia coli  yahK (NP_414859.1),  Escherichia coli  ybbO (NP_415026.1),  Escherichia coli  ybdH (NP_415132.1),  Escherichia coli  yiaY (YP_026233.1),  Escherichia coli  yjgB (NP_418690.4), or homologues thereof. 
     
     
         81 . The microorganism of  claim 19 , wherein said overexpressed aldehyde dehydrogenase is encoded by  Escherichia coli  aldA (P25553),  Escherichia coli  aldB (P37685),  Escherichia coli  punC (P23883),  Pseudomonas putida  alkH (Q9WWW3),  Klebsiella pneumoniae  KPN_01018 (A6T782),  Rhodococcus erythropolis  aldhR (Q4F895), or homologues thereof. 
     
     
         82 . The microorganism of  claim 19 , wherein said overexpressed acyl-CoA synthetase is encoded by  Escherichia coli  fadD (P69451),  Escherichia coli  fadK (P38135),  Pseudomonas putida  alkK (Q9L4M6), or homologues thereof. 
     
     
         83 . The microorganism of  claim 19 , wherein said overexpressed acylating aldehyde dehydrogenase is encoded by  E. coli  mhpF (NP_414885.1),  Pseudomonas  sp. CF600 drnpF (Q52060), or homologues thereof. 
     
     
         84 . The microorganism of  claim 20 , wherein said overexpressed acyl-CoA dehydrogenase is encoded by  Escherichia coli  fadE (AP_000876.1), or homologues thereof. 
     
     
         85 . The microorganism of  claim 10 , wherein said overexpressed enoyl-CoA hydratase encoded by  Escherichia coli  fadB (NP_418288.1), or homologues thereof. 
     
     
         86 . The microorganism of  claim 10 , wherein said overexpressed 3-hydroxyacyl-CoA dehydrogenase is encoded by  Escherichia coli  fadB (NP_418288.1), or homologues thereof. 
     
     
         87 . The microorganism of  claim 10 , wherein said overexpressed thiolase is encoded by,  Escherichia coli  atoB (NP_416728.1),  Escherichia coli  yqeF (NP_417321.2),  Escherichia coli  fadA (YP_026272.1),  Escherichia coli  fadI (NP_416844.1), or homologues thereof. 
     
     
         88 . The microorganism of  claim 21 , wherein said overexpressed thiolase is encoded by  E. coli  atoB (NP_416728.1),  E. coli  yqeF (NP_417321.2),  E. coli  fadA (YP_026272.1),  E. coli  fadI (NP_416844.1),  Ralstonia eutropha  bktB (AAC38322.1),  Pseudomonas  sp. Strain B13 catF (AAL02407.1),  E. coli  paaJ (NP_415915.1),  Pseudomonas putida  pcaF (AAA85138.1),  Rhodococcus opacus  pcaF (YP_002778248.1),  Streptomyces  sp. pcaF (AAD22035.1),  Ralstonia eutropha  phaA (AEI80291.1),  Clostridium acetobutylicum  thIA (AAC26023.1), or  Clostridium acetobutylicum  thIB (AAC26026.1), or homologues thereof. 
     
     
         89 . The microorganism of  claim 21 , wherein said overexpressed 3-hydroxyacyl-CoA dehydrogenase or 3-oxoacyl-[acyl-carrier-protein] reductase is encoded by  E. coli  fadB (NP_418288.1),  E. coli  fadJ (NP_416843.1),  Ralstonia eutropha  phaB1 (YP_725942.1),  Ralstonia eutropha  phaB2 (YP_726470.1),  Ralstonia eutropha  phaB3 (YP_726636.1),  E. coli  paaH (P76083),  E. coli  fabG (NP_415611.1), or homologues thereof. 
     
     
         90 . The microorganism of  claim 21 , wherein said overexpressed enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydratase, or 3-hydroxyacyl-[acyl-carrier-protein] dehydratase is encoded by  E. coli  fadB (NP_418288.1),  E. coli  fadJ (NP_416843.1),  Aeromonas caviae  phaJ (032472.1),  Pseudomonas aeruginosa  phaJ1 (BAA92740.1),  Pseudomonas aeruginosa  phaJ2 (BAA92741.1),  Pseudomonas aeruginosa  phaJ3 (BAC44834.1),  Pseudomonas aeruginosa  phaJ4 (BAC44835.1),  E. coli  paaF (P76082),  E. coli  fabA (NP_415474.1),  E. coli  fabZ (NP_414722.1), or homologues thereof. 
     
     
         91 . The microorganism of  claim 21 , wherein said trans-enoyl-CoA reductase or enoyl-[acyl-carrier-protein] reductase is encoded by  E. coli  ydiO (P0A9U8),  Euglena gracilis  egTER (Q5EU90.1),  Treponema denticola  tdTER (NP_971211.1),  E. coli  fabI (NP_415804.1),  Enterococcus faecalis  fabK (NP_816503.1),  Bacillus subtilis  fabL (KFK80655.1),  Vibrio cholerae  fabV (ABX38717.1), or homologues thereof. 
     
     
         92 . The microorganism of  claim 22 , wherein said overexpressed acetyl-CoA carboxylase is encoded by  E. coli  accABCD (P0ABD5, P0ABD8, P24182, P0A9Q5), or homologues thereof. 
     
     
         93 . The microorganism of  claim 22 , wherein said overexpressed malonyl-CoA-ACP transacylase is encoded by  E. coli  fabD (P0AAI9), or homologues thereof. 
     
     
         94 . The microoroganism of  claim 22 , wherein said overexpressed β-ketoacyl-ACP synthase is encoded by  E. coli  fabB (P0A953),  E. coli  fabF (P0AAI5),  E. coli  fabH (P0A6R0), or homologues thereof. 
     
     
         95 . The microorganism of  claim 22 , wherein said overexpressed 3-oxoacyl-[acyl-carrier-protein] reductase is encoded by  E. coli  fabG (NP_415611.1), or homologues thereof. 
     
     
         96 . The microorganism of  claim 22 , wherein said overexpressed 3-hydroxyacyl-[acyl-carrier-protein] dehydratase is encoded by  E. coli  fabA (NP_415474.1),  E. coli  fabZ (NP_414722.1), or homologues thereof. 
     
     
         97 . The microorganism of  claim 22 , wherein said enoyl-[acyl-carrier-protein] reductase is encoded by  E. coli  fabI (NP_415804.1),  Enterococcus faecalis  fabK (NP_816503.1),  Bacillus subtilis  fabL (KFK80655.1),  Vibrio cholerae  fabV (ABX38717.1), or homologues thereof. 
     
     
         98 . The microorganism of  claim 23 , wherein said overexpressed thioesterase is encoded by  E. coli  tesA (NP_415027.1),  E. coli  tesB (NP_414986.1),  E. coli  yciA (NP_415769.1),  E. coli  (NP_414977.1),  E. coli  ydiI (NP_416201.1),  E. coli  ybgC (NP_415264.1),  Alcanivorax borkumensis  tesB2 (YP_692749.1)  Fibrobacter succinogenes  Fs2108 (YP_005822012.1),  Prevotella ruminicola  Pr655 (YP_003574018.1)  Prevotella ruminicola  Pr1687 (YP_003574982.1), or homologues thereof. 
     
     
         99 . The microorganism of  claim 23 , wherein said overexpressed acyl-CoA:acetyl-CoA transferase is encoded by  E. coli  atoD (NP_416725.1),  Clostridium kluyveri  call (AAA92344.1),  Clostridium acetobutylicum  ctfAB (NP_149326.1, NP_149327.1) or  E. coli  ydiF (NP_416209.1), or homologues thereof. 
     
     
         100 . The microorganism of  claim 23 , wherein said overexpressed phosphotransacylase is encoded by  Clostridium acetobutylicum  ptb (NP_349676.1),  Enterococcus faecalis  ptb (AAD55374.1),  Salmonella enterica  pduL (AAD39011.1), or homologues thereof. 
     
     
         101 . The microorganism of  claim 23 , wherein said overexpressed carboxylate kinase is encoded by  Clostridium acetobutylicum  buk (AAK81015.1),  Enterococcus faecalis  buk (AAD55375.1),  Salmonella enterica  pduW (AAD39021.1), or homologues thereof. 
     
     
         102 . The microorganism of  claim 24 , wherein said overexpressed ACP-cleaving thioesterase is encoded by  E. coli  tesA (NP_415027.1),  Cuphea palustris  fatB1 (AAC49179.1),  Cuphea viscosissima  fatB3 (AEM72524.1),  Ulmus americana  fatB1 (AAB71731.1),  Cocos nucifera  fatB2 (AEM72520.1),  Elaeis guineensis  PTE (AAD42220.2),  Clostridium perfringens  CPF 2954 (ABG82470.1),  Umbellularia californica  fatB1 (AAA34215.1), or homologues thereof. 
     
     
         103 . The microorganism of  claim 26 , wherein said overexpressed alcohol-forming coenzyme-A thioester reductase is encoded by  Clostridium acetobutylicum  adhE2 (YP_009076789.1),  Arabidopsis thaliana  At3g11980 (AEE75132.1),  Arabidopsis thaliana  At3g44560 (AEE77915.1),  Arabidopsis thaliana  At3g56700 (AEE79553.1),  Arabidopsis thaliana  At5g22500 (AED93034.1),  Arabidopsis thaliana  CER4 (AEE86278.1),  Marinobacter aquaeolei  VT8 maqu_2220 (VP_959486.1),  Marinobacter aquaeolei  VT8 maqu_2507 (YP_959769.1), or homologues thereof. 
     
     
         104 . The microorganism of  claim 26  or  29 , wherein said overexpressed aldehyde-forming CoA thioester reductase is encoded by  Acinetobacter calcoaceticus  acr1 (AAC45217.1),  Acinetobacter  sp Strain M-1 acrM (BAB85476.1),  Clostridium beijerinckii  ald (AAT66436.1),  E. coli  eutE (NP_416950.1),  Salmonella enterica  eutE (AAA80209.1),  E. coli  mhpF (NP_414885.1), or homologues thereof. 
     
     
         105 . The microorganism of  claim 27 , wherein said overexpressed alcohol-forming ACP thioester reductase is encoded by  Marinobacter aquaeolei  VT8 maqu_2220 (VP_959486.1),  Hahella chejuensis  hch_05075 (ABC31758.1),  Marinobacter algicola  MDG893_11561 (A6EVI7),  Bermanella marisrubri  RED65_09894 (Q1N697), or homologues thereof. 
     
     
         106 . The microorganism of  claim 27  or  30 , wherein said overexpressed aldehyde-forming ACP thioester reductase is encoded by  Nostoc punctiforme  Npun_R1710 (ACC80381.1),  Synechococcus elongates  Synpcc7942_1594 (Q54765),  Prochlorococcus marinus  P9515_05971 (A2BVJ5),  Synechocystis  sp. PCC 6803 sll0209 (YP_005652204.1), or homologues thereof. 
     
     
         107 . The microorganism of  claim 26  or  27 , wherein said overexpressed alcohol dehydrogenase is encoded by  E. coli  betA (NP_414845.1),  E. coli  dkgA (NP_417485.4),  E. coli  eutG (NP_416948.4),  E. coli  fucO (NP_417279.2),  E. coli  ucpA (NP_416921.4),  E. coli  yahK (NP_414859.1),  E. coli  ybbO (NP_415026.1),  E. coli  ybdH (NP_415132.1),  E. coli  yiaY (YP_026233.1),  E. coli  yjgB (NP_418690.4), or homologues thereof. 
     
     
         108 . The microorganism of  claim 29  or  30 , wherein said overexpressed aldehyde decarbonylase is encoded by  Synechococcus elongates  PCC7942 orf1593 (Q54764.1),  Nostoc punctiforme  PCC73102 npun_R1711 (B2J1M1.1),  Prochlorococcus marinus  MIT9313 pmt1231 (Q7V6D4.1), or homologues thereof. 
     
     
         109 . The microorganism of  claim 32 ,  33 , or  39 , wherein said overexpressed transaminase is encoded by  Arabidopsis thaliana  At3g22200 (NP_001189947.1),  Alcaligenes denitrificans  aptA (AAP_92672.1),  Bordetella bronchiseptica  BB0869 (WP_015041039.1),  Bordetella parapertussis  BPP0784 (WP_010927683.1),  Brucella melitensis  BAWG 0478 (EEW88370.1),  Burkholderia pseudomallei  BP1026B_I0669 (AFI65333.1),  Chromobacterium violaceum  CV2025 (AAQ59697.1),  Oceanicola granulosus  OG2516_07293 (WP_007254984.1),  Paracoccus denitrificans  PD1222 Pden 3984 (ABL72050.1),  Pseudogulbenkiania ferrooxidans  ω-TA (WP_008952788.1),  Pseudomonas putida  ω-TA (P28269.1),  Ralstonia solanacearum  ω-TA (YP_002258353.1),  Rhizobium meliloti  SMc01534 (NP_386510.1), and  Vibrio fluvialis  ω-TA (AEA39183.1),  Mus musculus  abaT (AAH58521.1)  E. coli  gabT (YP_490877.1), or homologues thereof. 
     
     
         110 . The microorganism of  claims 35 - 41 , wherein said overexpressed carboxylic acid omega hydroxylase is encoded by  Pseudomonas putida  alkBGT (YP_009076004.1, Q9WWW4.1, Q9L4M8.1),  Marinobacter aquaeolei  CYP_153A (ABM17701.1),  Mycobacterium marinum  CYP_153A16 (YP_001851443.1),  Polaromonas  sp. CYP_153A (YP_548418.1),  Nicotiana tabacum  CYP94A5 (AAL54887.1),  Vicia sativa  CYP94A1 (AAD10204.1),  Vicia sativa  CYP94A2 (AAG33645.1),  Arabidopsis thaliana  CYP94B1 (BAB08810.1),  Arabidopsis thaliana  CYP86A8 (CAC67445.1),  Candida tropicalis  CYP52A1 (AAA63568.1, AAA34354.1, AAA34334.1),  Candida tropicalis  CYP52A2 (AAA34353.2, CAA35593.1),  Homo sapiens  CYP4A11 (AAQ56847.1), or homologues thereof. 
     
     
         111 . The microorganism of  claim 36 ,  38 ,  39 , or  41 , wherein said overexpressed alcohol oxidase is encoded by  Rhodococcus ruber  SC1 cddC (AAL14237.1),  Acinetobacter  sp. SE19 chnD (AAG10028.1),  E. coli  yahK (NP_414859.1),  E. coli  yjgB (NP_418690.4), or homologues thereof. 
     
     
         112 . The microorganism of  claim 36 ,  38 , or  41 , wherein said overexpressed aldehyde dehydrogenase is encoded by  Rhodococcus ruber  SC1 cddD (AAL14238.1),  Acinetobacter  sp. SE19 chnE (AAG10022.1), or homologues thereof. 
     
     
         113 . The microorganism of  claim 42 ,  43 , or  44 , wherein said overexpressed fatty acid alpha hydroxylases is encoded by  Myxococcus xanthus  MXAN_0191 (YP_628473.1),  Stigmatella aurantiaca  STIAU_3334 (YP_003957653.1), or homologues thereof. 
     
     
         114 . The microorganism of  claim 45 , wherein said reduced expression of fermentation enzymes are ΔadhE, (Δpta or ΔackA or ΔackApta), ΔpoxB, ΔldhA, and ΔfrdA and less acetate, lactate, ethanol and succinate are thereby produced. 
     
     
         115 . A method of a product comprising growing a genetically engineered microorganism or recombinant bacteria according to any of  claims 1 - 114  in a culture broth containing an alkane as the sole carbon source, activating said alkane, generating precursor intermediate acetyl-CoA, producing a product from said acetyl-CoA, and isolating said product. 
     
     
         116 . A method of a product comprising growing a genetically engineered microorganism or recombinant bacteria according to any of  claims 1 - 114  in a culture broth containing an alkane as the sole carbon source and a terminal electron acceptor (such as SO 4   2− , NO 3   − , Fe 3+ , O 2 , Mn 4+ ), activating said alkane, generating precursor intermediate acetyl-CoA, producing a product from said acetyl-CoA, and isolating said product.

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