Disorders of oxalate metabolism

The invention provides a non-naturally occurring microbial organism having an adipate, 6-aminocaproic acid or caprolactam pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective adipate, 6-aminocaproic acid or caprolactam pathway. The invention additionally provides a method for producing adipate, 6-aminocaproic acid or caprolactam. The method can include culturing an adipate, 6-aminocaproic acid or caprolactam producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding an adipate, 6-aminocaproic acid or caprolactam pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce adipate, 6-aminocaproic acid or caprolactam.

Microorganisms for the production of adipic acid and other compounds

The invention provides a non-naturally occurring microbial organism having an acetyl-CoA pathway and the capability of utilizing syngas or syngas and methanol. In one embodiment, the invention provides a non-naturally occurring microorganism, comprising one or more exogenous proteins conferring to the microorganism a pathway to convert CO, CO2 and/or H2 to acetyl-coenzyme A (acetyl-CoA), methyl tetrahydrofolate (methyl-THF) or other desired products, wherein the microorganism lacks the ability to convert CO or CO2 and H2 to acetyl-CoA or methyl-THF in the absence of the one or more exogenous proteins. For example, the microbial organism can contain at least one exogenous nucleic acid encoding an enzyme or protein in an acetyl-CoA pathway. The microbial organism is capable of utilizing synthesis gases comprising CO, CO2 and/or H2, alone or in combination with methanol, to produce acetyl-CoA. The invention additionally provides a method for producing acetyl-CoA, for example, by culturing an acetyl-CoA producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding an acetyl-CoA pathway enzyme or protein in a sufficient amount to produce acetyl-CoA, under conditions and for a sufficient period of time to produce acetyl-CoA.

Methods and organisms for utilizing synthesis gas or other gaseous carbon sources and methanol

A non-naturally occurring microbial organism having an isopropanol, 4-hydroxybutryate, or 1,4-butanediol pathway includes at least one exogenous nucleic acid encoding an isopropanol, 4-hydroxybutryate, or 1,4-butanediol pathway enzyme expressed in a sufficient amount to produce isopropanol, 4-hydroxybutryate, or 1,4-butanediol. The aforementioned organisms are cultured to produce isopropanol, 4-hydroxybutryate, or 1,4-butanediol.

Microorganisms and methods for conversion of syngas and other carbon sources to useful products

The invention provides a non-naturally occurring microbial organism having a 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway. The invention additionally provides a method for producing 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid. The method can include culturing a 6-aminocaproic acid, caprolactam or hexametheylenediamine producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding a 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid.

Microorganisms and methods for the biosynthesis of adipate, hexamethylenediamine and 6-aminocaproic acid

https://science.sciencemag.org/content/sci/150/3703/1548.full.pdf

Glyoxylate in Fatty-Acid Metabolism

Megraw, Robert E (Albert Einstein Medical Center, Philadelphia, Pa), Henry C Reeves, and Samuel J Ajl Formation of lactyl-coenzyme A and pyruvyl-coenzyme A from lactic acid by Escherichia coli J Bacteriol 90:984-988 1965-Cell extracts of propionate-adapted Escherichia coli were found to contain a lactyl-coenzyme A (CoA) synthetase which catalyzes the formation of the CoA thiolester from lactate, CoA, and cofactors The extracts also catalyzed the nicotinamide adenine dinucleotide-dependent oxidation of lactyl-CoA The product of this oxidation was identified chromatographically as pyruvyl-CoA

Formation of Lactyl-Coenzyme A and Pyruvyl-Coenzyme A from Lactic Acid by Escherichia coli

Interference by ethanol in the oxidation of CoA esters

WHILE attempting to isolate and identify pyridme nucleotide-dependent and enzymatically-formed aldehydes and α-keto acids as their 2,4-dinitrophenylhydrazone derivatives, it was noted that derivatives were formed which, when chromatographed on paper, were unlike known standards and gave blue colours when sprayed with alcoholic KOH. The reaction mixture in which this phenomenon was first observed was a control tube that contained: tris-HCl buffer, pH 8.5, 1,500 µmoles; nicotinamide-adenine-dinucleotide (NAD), 10.0 µmoles; and crude cell-free extract containing 1.2 mg protein in a total volume of 3.8 ml. The incubation was terminated by the addition of an equal volume of saturated 2,4-dinitrophenylhydrazine (DNPH) in 2 N HCl. The reaction mixture was centrifuged to remove precipitated protein and the supernatant fluid decanted into a clean test-tube and incubated overnight at 37° C. Further investigations revealed that the flocculent precipitate which formed was due to a reaction between NAD and DNPH. This product was purified by the usual extraction procedure including initial extraction with ethyl acetate to remove unreacted DNPH, neutral and acidic hydrazones; the latter were re-extracted into 10 per cent sodium carbonate, leaving unreacted DNPH and neutral hydrazones behind in the organic phase; the carbonate layer was acidified at 4° C and re-extracted with ethyl acetate. The ethyl acetate layer was evaporated and aliquots were used for spotting on to paper chromatograms.

Reaction of pyridine nucleotides with 2,4-dinitrophenylhydrazine.

MEGRAW,ROBERTE.(Albert Einstein MedicalCenter, Philadelphia, Pa.), HENRYC. REEVES, AND SAMUELJ.AJL.Formation oflactyl-coenzyme A andpyruvyl-coenzyme A fromlactic acidbyEscherichia coli. J.Bacteriol. 90:984-988. 1965.-Cell extracts of propionate-adapted Escherichia coli were foundtocontain a lactyl-coenzyme A (CoA) synthetase whichcatalyzes theformation oftheCoAthiolester fromlactate, CoA,and cofactors. Theextracts alsocatalyzed thenicotinamide adenine dinucleotide-dependent oxidation oflactyl-CoA. Theproduct ofthisoxidation was identified chromatographically aspyruvyl-CoA. ReevesandAjl(1962) reported thatcell extracts of propionate-grown Escherichia coli, strain E-26contain anenzyme whichcatalyzes a 3-condensation ofpropionyl-coenzyme A (CoA) andglyoxylate toyield a-hydroxyglutarate. It wassubsequently notedthatthese extracts contained anenzymewhichwouldcleave thisahydroxy acid toyield lactate andacetate (Reeves andAjl, 1963). Stoichiometric quantities ofacetatewererecovered, butconsiderably less than theoretical amountsoflactate wererecovered, suggesting thatlactate wasbeing metabolized further. Further investigations revealed that lactate, astheCoAthiolester, wasbeing converted tohydroxypyruvic aldehyde (Reeves and Ajl, 1965a). We began thepresent study onthe premise thatthemetabolism oflactyl-CoA to pyruvyl-CoA wasthefirst reaction totakeplace inthis metabolic series. Inthis communication, wereport thatthis reaction doesindeed occur, andthatthese sameextracts contain anenzyme thatcatalyzes thesynthesis oflactyl-CoA from lactate andCoA.We havenamedthis enzyme lactyl-CoA synthetase (Commission onEnzymes, 1961).

Formation ofLactyl-Coenzyme A andPyruvyl- Coenzyme A fromLactic Acidby Escherichia coli

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