Aminomuconate semialdehyde dehydrogenase. Medical search

An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).

Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.

An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.

An NAD+ dependent enzyme that catalyzes the oxidation of 2-aminomuconate 6-semialdehyde to 2-aminomuconate.

Oxidoreductases that are specific for ALDEHYDES.

An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.

Phenols substituted in any position by an amino group.

Brain disorders resulting from inborn metabolic errors, primarily from enzymatic defects which lead to substrate accumulation, product reduction, or increase in toxic metabolites through alternate pathways. The majority of these conditions are familial, however spontaneous mutation may also occur in utero.

An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.

The sodium salt of 4-hydroxybutyric acid. It is used for both induction and maintenance of ANESTHESIA.

Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.

An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.

An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.

Salts and esters of hydroxybutyric acid.

Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.

Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.

A species of motile, free-living, gram-negative bacteria that occur in the soil. They are aerobic or microaerophilic and are sometimes capable of nitrogen fixation.

The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.

The most common inhibitory neurotransmitter in the central nervous system.

A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

Organic compounds containing a carbonyl group in the form -CHO.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.

Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

The rate dynamics in chemical or physical systems.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

The functional hereditary units of BACTERIA.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

An essential amino acid. It is often added to animal feed.

A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.

Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.

A metabolite in the principal biochemical pathway of lysine. It antagonizes neuroexcitatory activity modulated by the glutamate receptor, N-METHYL-D-ASPARTATE; (NMDA).

A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.

An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.

In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.

Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.

Proteins found in any species of bacterium.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.

D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.

Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.

Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.

Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.

A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.

An enzyme that catalyzes the oxidation of 3-oxopropanoate (malonate semialdehyde) to acetyl COENZYME A. It plays a role in the metabolism of BETA-ALANINE.

An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.

Alcohol oxidoreductases with substrate specificity for LACTIC ACID.

A group of 1,2-benzenediols that contain the general formula R-C6H5O2.

An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.

Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.

A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.

An order of CRENARCHAEOTA consisting of aerobic or facultatively aerobic, chemolithotrophic cocci which are extreme thermoacidophiles. They lack peptidoglycan in their cell walls.

A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.

A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.

The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).

Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.

The 4-aminomethyl form of VITAMIN B 6. During transamination of amino acids, PYRIDOXAL PHOSPHATE is transiently converted into pyridoxamine phosphate.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.

Oxidoreductases that are specific for KETONES.

An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.

An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.

A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.

Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.

A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.

A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.

An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.

A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.

Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.

Non-heme iron-containing enzymes that incorporate two atoms of OXYGEN into the substrate. They are important in biosynthesis of FLAVONOIDS; GIBBERELLINS; and HYOSCYAMINE; and for degradation of AROMATIC HYDROCARBONS.

Catalyzes the oxidation of catechol to 2-hydroxymuconate semialdehyde in the carbazole and BENZOATE degradation via HYDROXYLATION pathways. It also catalyzes the conversion of 3-methylcatechol to cis, cis-2-hydroxy-6-oxohept-2,4-dienoate in the TOLUENE and XYLENE degradation pathway. This enzyme was formerly characterized as EC 1.13.1.2.

Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.

A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.

Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.

An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. It was formerly characterized as EC 1.13.1.6.

Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure.

A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).

A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)

An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.

Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde. (1/2)

Pseudomonas pseudoalcaligenes JS45 utilizes nitrobenzene as the sole source of nitrogen, carbon, and energy. Previous studies have shown that degradation of nitrobenzene involves the reduction of nitrobenzene to nitrosobenzene and hydroxylaminobenzene, followed by rearrangement to 2-aminophenol, which then undergoes meta ring cleavage to 2-aminomuconic semialdehyde. In the present paper, we report the enzymatic reactions responsible for the release of ammonia after ring cleavage. 2-Aminomuconic semialdehyde was oxidized to 2-aminomuconate in the presence of NAD by enzymes in crude extracts. 2-Aminomuconate was subsequently deaminated stoichiometrically to 4-oxalocrotonic acid. No cofactors are required for the deamination. Two enzymes, 2-aminomuconic semialdehyde dehydrogenase and a novel 2-aminomuconate deaminase, distinguished by partial purification of the crude extracts, catalyzed the two reactions. 4-Oxalocrotonic acid was further degraded to pyruvate and acetaldehyde. The key enzyme, 2-aminomuconate deaminase, catalyzed the hydrolytic deamination that released ammonia, which served as the nitrogen source for growth of the organism. (+info)

Purification, characterization, and sequence analysis of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas pseudoalcaligenes JS45. (2/2)

2-Aminonumconic 6-semialdehyde is an unstable intermediate in the biodegradation of nitrobenzene and 2-aminophenol by Pseudomonas pseudoalcaligenes JS45. Previous work has shown that enzymes in cell extracts convert 2-aminophenol to 2-aminomuconate in the presence of NAD+. In the present work, 2-aminomuconic semialdehyde dehydrogenase was purified and characterized. The purified enzyme migrates as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a molecular mass of 57 kDa. The molecular mass of the native enzyme was estimated to be 160 kDa by gel filtration chromatography. The optimal pH for the enzyme activity was 7.3. The enzyme is able to oxidize several aldehyde analogs, including 2-hydroxymuconic semialdehyde, hexaldehyde, and benzaldehyde. The gene encoding 2-aminomuconic semialdehyde dehydrogenase was identified by matching the deduced N-terminal amino acid sequence of the gene with the first 21 amino acids of the purified protein. Multiple sequence alignment of various semialdehyde dehydrogenase protein sequences indicates that 2-aminomuconic 6-semialdehyde dehydrogenase has a high degree of identity with 2-hydroxymuconic 6-semialdehyde dehydrogenases. (+info)

Other names in common use include 2-aminomuconate semialdehyde dehydrogenase, 2-hydroxymuconic acid semialdehyde dehydrogenase ... an aminomuconate-semialdehyde dehydrogenase (EC 1.2.1.32) is an enzyme that catalyzes the chemical reaction 2-aminomuconate 6- ... alpha-hydroxymuconic epsilon-semialdehyde dehydrogenase, and 2-hydroxymuconic semialdehyde dehydrogenase. Ichiyama A, Nakamura ... 2-hydroxymuconate semialdehyde dehydrogenase, alpha-aminomuconic epsilon-semialdehyde dehydrogenase, ...

https://en.wikipedia.org/wiki/Aminomuconate-semialdehyde_dehydrogenase

... oxidizing 2-aminomuconate semialdehyde to 2-aminomuconic acid. Two transcript variants encoding distinct isoforms have been ... Aldehyde dehydrogenase 8 family, member A1 also known as ALDH8A1 is an enzyme that in humans is encoded by the ALDH8A1 gene. ... This protein belongs to the aldehyde dehydrogenase family of enzymes. It was originally thought to play a role in a pathway of ... Davis I, Yang Y, Wherritt D, Liu A (June 2018). "Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the ...

https://en.wikipedia.org/wiki/ALDH8A1

... aminomuconate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.374 - aspartate-semialdehyde dehydrogenase MeSH D08.811. ... succinate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.875 - succinate-semialdehyde dehydrogenase (NAD(P)+) MeSH D08.811 ... l-aminoadipate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.812 - malonate-semialdehyde dehydrogenase (acetylating) MeSH ... betaine-aldehyde dehydrogenase MeSH D08.811.682.657.163.562 - glutamate-5-semialdehyde dehydrogenase MeSH D08.811.682.657. ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

L-aminoadipate-semialdehyde dehydrogenase EC 1.2.1.32: aminomuconate-semialdehyde dehydrogenase EC 1.2.1.33: (R)- ... IMP dehydrogenase EC 1.2.1.15: malonate-semialdehyde dehydrogenase EC 1.2.1.16: succinate-semialdehyde dehydrogenase [NAD(P)+] ... glutarate-semialdehyde dehydrogenase EC 1.2.1.21: glycolaldehyde dehydrogenase EC 1.2.1.22: lactaldehyde dehydrogenase EC 1.2. ... succinate-semialdehyde dehydrogenase (acylating) EC 1.2.1.77: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) EC 1.2. ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)

2-hydroxymuconate-semialdehyde hydrolase EC 3.7.1.10: cyclohexane-1,3-dione hydrolase EC 3.7.1.11: cyclohexane-1,2-dione ... 2-aminomuconate deaminase (2-hydroxymuconate-forming) * *No Wikipedia article EC 3.6.1.1: inorganic diphosphatase EC 3.6.1.2: ... pyruvate dehydrogenase (acetyl-transferring)]-phosphatase EC 3.1.3.44: [acetyl-CoA carboxylase]-phosphatase EC 3.1.3.45: 3- ... 2-aminomuconate deaminase (2-hydroxymuconate-forming) * *No Wikipedia article EC 3.6.1.1: inorganic diphosphatase EC 3.6.1.2: ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)

Aminomuconate-semialdehyde dehydrogenase Synonymes. 2-AMS dehydrogenase 2-Aminomuconic 6-semialdehyde dehydrogenase ... 2-AMS dehydrogenase. 2-Aminomuconic 6-semialdehyde dehydrogenase. Aminomuconate-semialdéhyde déshydrogénase. Code(s) ... Methylmalonate-semialdehyde dehydrogenase (acylating) [D08.811.682.657.163.827] Methylmalonate-semialdehyde dehydrogenase ( ... Aminomuconate-semialdehyde dehydrogenase - Concept préféré Concept UI. M0285718. Terme préféré. ...

https://decs.bvsalud.org/fr/ths/resource/?id=50610

Aminomuconate-semialdehyde dehydrogenase (substance). Code System Preferred Concept Name. Aminomuconate-semialdehyde ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=42242004

2-amino-3-carboxymuconate-6-semialdehyde decarboxylase. nbaE. 2-aminomuconate 6-semialdehyde dehydrogenase. Shew_3574. Shew_ ... 2-aminomuconate semialdehyde, a dehydrogenase forms (2Z,4E)-2-aminomuconate, a deaminase forms (3E)-2-oxo-3-hexenedioate (also ... acetaldehyde dehydrogenase (not acylating). Shew_3574. Shew_1910. ald-dh-CoA. acetaldehyde dehydrogenase, acylating. Shew_1910 ... 2-hydroxymuconate semialdehyde hydrolase. Confidence: high confidence medium confidence low confidence. transporter - ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__PV4&path=tryptophan

2 Aminomuconic 6 Semialdehyde Dehydrogenase use Aminomuconate-Semialdehyde Dehydrogenase 2 Aminonaphthalene use 2-Naphthylamine ... 2-Aminomuconic 6-Semialdehyde Dehydrogenase use Aminomuconate-Semialdehyde Dehydrogenase 2-Aminonaphthalene use 2-Naphthylamine ... 3 Isopropylmalate Dehydrogenase use 3-Isopropylmalate Dehydrogenase 3 Keto 5 alpha Steroid delta 4 Dehydrogenase use 3-Oxo-5- ... 3 Hydroxyacyl CoA Dehydrogenases use 3-Hydroxyacyl CoA Dehydrogenases 3 Hydroxyacyl CoA Dehydrogenase use 3-Hydroxyacyl-CoA ...

https://decs.bvs.br/I/DeCS2017_Alfab-0a9.htm

2-Aminomuconic 6-semialdehyde dehydrogenase (AmnC), a member of the aldehyde dehydrogenase (ALDH) superfamily, is responsible ... for oxidizing 2-aminomuconic 6-semialdehyde to 2-aminomuconate. In contrast to many other members of the ALDH superfamily, the ... The tetrameric assembly of 2-aminomuconic 6-semialdehyde dehydrogenase is a functional requirement of cofactor NAD+ binding. ... of AmnC dramatically lose NAD+ binding affinity and failed to oxidize the substrate analogue 2-hydroxymuconate-6-semialdehyde ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=au:Zhong,+Zhihui

https://decs2020.bvsalud.org/I/DeCS2016_Alfab-0a9.htm

https://decs2019.bvsalud.org/I/DeCS2017_Alfab-0a9.htm

https://decs2018.bvsalud.org/I/DeCS2018_Alfab-0a9.htm

https://decs2017.bvsalud.org/I/DeCS2017_Alfab-0a9.htm

1.2.1.32 aminomuconate-semialdehyde dehydrogenase - MetaCyc: RXN-8837 2-amino-5-chloromuconate + H2O + H+ <=> 5-chloro-2- ... 2-amino-5-chlorophenol + O2 <=> 2-amino-5-chloromuconate_6-semialdehyde + H+ 1.13.11.76 2-amino-5-chlorophenol 1,6-dioxygenase ... 2-amino-5-chloromuconate_6-semialdehyde + NAD+ + H2O <=> 2-amino-5-chloromuconate + NADH + H+ ...

https://mmtb.tu-bs.de/pathway/name/4-chloronitrobenzene%20degradation

Aminomuconate-Semialdehyde Dehydrogenase [D08.811.682.657.163.342] * Aspartate-Semialdehyde Dehydrogenase [D08.811.682.657. ... Succinate-Semialdehyde Dehydrogenase [D08.811.682.657.163.843] * Succinate-Semialdehyde Dehydrogenase (NADP+) [D08.811.682.657. ... L-Aminoadipate-Semialdehyde Dehydrogenase [D08.811.682.657.163.796] * Malonate-Semialdehyde Dehydrogenase (Acetylating) [ ... Glutamate-5-Semialdehyde Dehydrogenase [D08.811.682.657.163.562] * Glyceraldehyde-3-Phosphate Dehydrogenases [D08.811.682.657. ...

https://meshb-prev.nlm.nih.gov/record/ui?ui=D050604

Aminomuconate-Semialdehyde Dehydrogenase. *Aspartate-Semialdehyde Dehydrogenase. *Benzaldehyde Dehydrogenase (NADP+). *Betaine- ... "Retinal Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Retinal Dehydrogenase" by people in this website by year, and ... Below are the most recent publications written about "Retinal Dehydrogenase" by people in Profiles. ...

https://profiles.jefferson.edu/display/28811

Aminomuconate-Semialdehyde Dehydrogenase. *Aspartate-Semialdehyde Dehydrogenase. *Benzaldehyde Dehydrogenase (NADP+). *Betaine- ... "Glutamate-5-Semialdehyde Dehydrogenase" by people in this website by year, and whether "Glutamate-5-Semialdehyde Dehydrogenase ... "Glutamate-5-Semialdehyde Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, ... Below are the most recent publications written about "Glutamate-5-Semialdehyde Dehydrogenase" by people in Profiles. ...

https://researchers.childrensmercy.org/display/25736

2-aminomuconate semialdehyde dehydrogenase (EC 1.2.1.32)@^fig,[email protected]~Metabolism of Aromatic [email protected]^Metabolism ... Respiratory dehydrogenases 1 (20). Formate dehydrogenase (3). Succinate dehydrogenase (5). Mitochondrial electron transport ... Dehydrogenase [email protected]^Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase complex (EC 1.8.1.4)@^fig,[email protected]~ ... Dehydrogenase [email protected]^Dihydrolipoamide dehydrogenase of branched-chain alpha-keto acid dehydrogenase (EC 1.8.1.4)@^fig, ...

https://pubseed.theseed.org/FIG/seedviewer.cgi?page=Organism&organism=216591.1

M00013 Malonate semialdehyde pathway, propanoyl-CoA => acetyl-CoA [PATH:T30968_00410 T30968_00640 T30968_01200 T30968_01100]. ... M00149 Succinate dehydrogenase, prokaryotes [PATH:T30968_00190]. M00151 Cytochrome bc1 complex respiratory unit [PATH:T30968_ ... M00038 Tryptophan metabolism, tryptophan => kynurenine => 2-aminomuconate [PATH:T30968_00380 T30968_01100]. ... M00143 NADH dehydrogenase (ubiquinone) Fe-S protein/flavoprotein complex, mitochondria [PATH:T30968_00190]. ...

https://www.kegg.jp/kegg-bin/show_organism?menu_type=pathway_modules&org=T30968

2-aminomuconic semialdehyde dehydrogenase. QuickGO ontology. BLASTP. 577112. 577549. 438. 2-aminomuconate deaminase. QuickGO ...

http://pregi.bi.up.ac.za/pre_gi_gene.php?source_accession=NC_010645&gi_accession=NC_010645:558974

Aminomuconate-Semialdehyde Dehydrogenase [D08.811.682.657.163.342] * Aspartate-Semialdehyde Dehydrogenase [D08.811.682.657. ... Succinate-Semialdehyde Dehydrogenase [D08.811.682.657.163.843] * Succinate-Semialdehyde Dehydrogenase (NADP+) [D08.811.682.657. ... L-Aminoadipate-Semialdehyde Dehydrogenase [D08.811.682.657.163.796] * Malonate-Semialdehyde Dehydrogenase (Acetylating) [ ... 2-AMS Dehydrogenase Term UI T315720. LexicalTag ABX. ThesaurusID NLM (2006). 2-Aminomuconic 6-Semialdehyde Dehydrogenase Term ...

https://meshb.nlm.nih.gov/record/ui?ui=D050648

Aminomuconate-Semialdehyde Dehydrogenase [D08.811.682.657.163.342] * Aspartate-Semialdehyde Dehydrogenase [D08.811.682.657. ... Succinate-Semialdehyde Dehydrogenase [D08.811.682.657.163.843] * Succinate-Semialdehyde Dehydrogenase (NADP+) [D08.811.682.657. ... L-Aminoadipate-Semialdehyde Dehydrogenase [D08.811.682.657.163.796] * Malonate-Semialdehyde Dehydrogenase (Acetylating) [ ... 2-AMS Dehydrogenase Term UI T315720. LexicalTag ABX. ThesaurusID NLM (2006). 2-Aminomuconic 6-Semialdehyde Dehydrogenase Term ...

https://meshb-prev.nlm.nih.gov/record/ui?ui=D050648

succinic semialdehyde dehydrogenase (RefSeq). 2-aminomuconate 6-semialdehyde dehydrogenase (EC 1.2.1.32) (characterized). 35%. ... aldehyde dehydrogenase (RefSeq). 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase ... 2-aminomuconate semialdehyde dehydrogenase (EC 1.2.1.32) (characterized). 39%. 99%. 357.1. Aldehyde dehydrogenase (EC 1.2.1.3) ... 3 candidates for nbaE: 2-aminomuconate 6-semialdehyde dehydrogenase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__PV4&path=tryptophan&step=nbaE

2-amino-3-carboxymuconate-6-semialdehyde decarboxylase. nbaE. 2-aminomuconate 6-semialdehyde dehydrogenase. CCNA_03243. CCNA_ ... 2-aminomuconate semialdehyde, a dehydrogenase forms (2Z,4E)-2-aminomuconate, a deaminase forms (3E)-2-oxo-3-hexenedioate (also ... 2-hydroxymuconate semialdehyde hydrolase. CCNA_02478. Confidence: high confidence medium confidence low confidence. transporter ... acetaldehyde dehydrogenase, acylating. andAa. anthranilate 1,2-dioxygenase (deaminating, decarboxylating), ferredoxin--NAD(+) ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__Caulo&path=tryptophan

Acids N0000170216 Aminolevulinic Acid N0000168171 Aminomethyltransferase N0000167901 Aminomuconate-Semialdehyde Dehydrogenase ... Succinate-CoA Ligases N0000167903 Succinate-Semialdehyde Dehydrogenase N0000167905 Succinate-Semialdehyde Dehydrogenase (NADP+ ... N0000167894 L-Aminoadipate-Semialdehyde Dehydrogenase N0000167967 L-Gulonolactone Oxidase N0000167971 L-Iditol 2-Dehydrogenase ... N0000167898 Glutamate-5-Semialdehyde Dehydrogenase N0000167771 Glutamate-Ammonia Ligase N0000167769 Glutamate-Cysteine Ligase ...

https://evs.nci.nih.gov/ftp1/FDA/ndfrt/Archive/StructuralClass%202012-06-04.txt

HN - 2006(1975) MH - Aminomuconate-Semialdehyde Dehydrogenase UI - D050648 MN - D8.811.682.657.163.342 MS - An NAD+ dependent ... Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-HYDROXYPROPIONIC ACID. HN ... HN - 2006 MH - Succinate-Semialdehyde Dehydrogenase UI - D050644 MN - D8.811.682.657.163.843 MS - An enzyme that plays a role ... HN - 2006(1974) MH - L-Aminoadipate-Semialdehyde Dehydrogenase UI - D050647 MN - D8.811.682.657.163.796 MS - An enzyme that ...

https://nlmpubs.nlm.nih.gov/projects/mesh/.newterms/.bkup/mshnew2006.10-03-2005.txt

Aminomuconate-semialdehyde dehydrogenase. AMANK. N-acetyl-D-mannosamine kinase. AMCOXO. 2-aminomuconate reductase ... Aldo-keto reductase family 1, member C1 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol ... Aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol ... Aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol ...

http://bigg.ucsd.edu/models/iMM1415/metabolites/h_c

... aminomuconate deaminase aminomuconate deaminases aminomuconic aminomuconic semialdehyde aminomuconic semialdehyde dehydrogenase ... magnesium hydrochlorides aspartatergic aspartates aspartate semialdehyde dehydrogenase aspartate semialdehyde dehydrogenases ... CoA dehydrogenase beta-hydroxyacyl CoA dehydrogenase beta hydroxyacyl CoA dehydrogenases beta-hydroxyacyl CoA dehydrogenases ... alpha-keto acid dehydrogenase branched-chain alpha-ketoacid dehydrogenase branched-chain alpha-keto acid dehydrogenase kinase ...

https://lexsrv3.nlm.nih.gov/LexSysGroup/Projects/gSpell/current/data/2006LexiconTerms.txt

https://decs.bvsalud.org/I/DeCS2018_Alfab-0a9.htm

Aminomuconate-Semialdehyde Dehydrogenase. *Aspartate-Semialdehyde Dehydrogenase. *Benzaldehyde Dehydrogenase (NADP+). *Betaine- ... L-Aminoadipate-Semialdehyde Dehydrogenase. *Malonate-Semialdehyde Dehydrogenase (Acetylating). *Methylmalonate-Semialdehyde ...

https://profiles.ouhsc.edu/display/19094

Aminocarboxymuconate-semialdehyde decarboxylase. *Aminomuconate-semialdehyde dehydrogenase. PHENYLALANINE→tyrosine→. *(see ...

https://www.knowpia.com/knowpedia/Melanin

2-aminomuconate_6-semialdehyde + NAD+ + H2O <=> 2-aminomuconate + NADH + H+ 1.2.1.32 aminomuconate-semialdehyde dehydrogenase - ... 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase - - - - - ... alpha-amino-beta-carboxymuconate-epsilon-semialdehyde + H+ <=> 2-aminomuconate_6-semialdehyde + CO2 4.1.1.45 ... 1.17.1.4 xanthine dehydrogenase 1.2.1.3 aldehyde dehydrogenase (NAD+) 1.2.1.39 phenylacetaldehyde dehydrogenase ...

https://mmtb.tu-bs.de/pathway/name/tryptophan%20metabolism

https://meshb-prev.nlm.nih.gov/record/ui?ui=D050727

https://lsg3.nlm.nih.gov/LexSysGroup/Projects/gSpell/current/data/2006LexiconTerms.txt

Aminomuconate-Semialdehyde Dehydrogenase Aminooxyacetic Acid Aminopeptidases Aminophenols Aminophylline Aminopropionitrile ... Acyl-CoA Dehydrogenase Acyl-CoA Dehydrogenase, Long-Chain Acyl-CoA Dehydrogenases Acyl-CoA Oxidase Acylation Acyltransferases ... 11-beta-Hydroxysteroid Dehydrogenase Type 1 11-beta-Hydroxysteroid Dehydrogenase Type 2 11-beta-Hydroxysteroid Dehydrogenases ... Aspartate-Semialdehyde Dehydrogenase Aspartate-tRNA Ligase Aspartic Acid Aspartic Acid Endopeptidases Aspartic Acid Proteases ...

https://nlmpubs.nlm.nih.gov/projects/mesh/.newterms/mshd2017.txt

Aminomuconate-Semialdehyde Dehydrogenase. *Aspartate-Semialdehyde Dehydrogenase. *Benzaldehyde Dehydrogenase (NADP+). *Betaine- ... "Glycolaldehyde Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Glycolaldehyde Dehydrogenase" by people in this website by ... Below are the most recent publications written about "Glycolaldehyde Dehydrogenase" by people in Profiles. ...

http://profiles.jefferson.edu/display/28779

1.2.1.32 aminomuconate-semialdehyde dehydrogenase 1.2.1.46 formaldehyde dehydrogenase 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] ... 1.2.1.22 lactaldehyde dehydrogenase 1.2.1.24 succinate-semialdehyde dehydrogenase (NAD+) 1.2.1.3 aldehyde dehydrogenase (NAD+) ... 1.2.1.65 salicylaldehyde dehydrogenase 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase - - - - - - - - - - BMK ... 1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) 1.2.1.8 betaine-aldehyde dehydrogenase - - - - ...

https://mmtb.tu-bs.de/search/formate%20=

... dehydrogenase ec: 1.2.1.32 aminomuconate-semialdehyde dehydrogenase ec: 1.2.1.36 retinal dehydrogenase ec: 1.2.1.39 ... dehydrogenase and CoA-dependent succinic semialdehyde dehydrogenase; CoA-dependent succinic semialdehyde dehydrogenase and ... 1.2.1.15 malonate-semialdehyde dehydrogenase ec: 1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)+] ec: 1.2.1.17 ... NADPH-dependant succinic semialdehyde dehydrogenase. In E. coli, gabD is an NADP-dependant succinic semialdehyde dehydrogenase ...

https://www.patentsencyclopedia.com/app/20090075351

Aminomuconate-semialdehyde dehydrogenase (substance) {42242004 , SNOMED-CT } Aryl-alcohol dehydrogenase (substance) {26753001 ... Glutamate-5-semialdehyde dehydrogenase (substance) {60943003 , SNOMED-CT } Glutarate-semialdehyde dehydrogenase (substance) { ... L-amino-acid dehydrogenase (substance) {3463001 , SNOMED-CT } L-Aminoadipate-semialdehyde dehydrogenase (substance) {32826004 ... Dehydrogenase Current Synonym true false 3520895011 Substance with dehydrogenase mechanism of action Current Synonym true false ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=129919009

Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be ... "pyruvate dehydrogenase kinase, isozyme 2 precursor" Pdk2 Rattus norvegicus " Inhibits the mitochondrial pyruvate dehydrogenase ... Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation. Q9Z2F5.3 ... the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, ...

https://esbl.nhlbi.nih.gov/helixweb/Database/Transcriptomic/images/ProximalTubuleData.txt

Enzyme that catalyzes the oxidation Succinic semialdehyde dehydrogenase Decarboxylase MetaCyc

An NAD + dependent enzyme that catalyzes the oxidation of 2-aminomuconate 6-semialdehyde to 2-aminomuconate. (bvsalud.org)
An enzyme that catalyzes the oxidation of succinate semialdehyde to SUCCINIC ACID . (nih.gov)
An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. (childrensmercy.org)

The invention provides a non-naturally occurring microbial biocatalyst including a microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway having at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce monomeric 4-hydroxybutanoic acid (4-HB). (patentsencyclopedia.com)
The method includes culturing a non-naturally occurring microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway including at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase or α-ketoglutarate decarboxylase under substantially anaerobic conditions for a sufficient period of time to produce monomeric 4-hydroxybutanoic acid (4-HB). (patentsencyclopedia.com)
2. The non-naturally occurring microbial biocatalyst of claim 1, wherein said 4-HB biosynthetic pathway comprises 4-hydroxybutanoate dehydrogenase and succinyl-CoA synthetase and CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase. (patentsencyclopedia.com)
6. The non-naturally occurring microbial biocatalyst of claim 3, further comprising a nucleic acid encoding an exogenous succinyl-CoA synthetase, exogenous CoA-dependent succinic semialdehyde dehydrogenase or exogenous succinyl-CoA synthetase and exogenous CoA-dependent succinic semialdehyde dehydrogenase. (patentsencyclopedia.com)
7. The non-naturally occurring microbial biocatalyst of claim 1, wherein said microbial organism lacks an endogenous 4-HB biosynthetic activity selected from 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, and α-ketoglutarate decarboxylase. (patentsencyclopedia.com)

Dioxygenase NbaC cleaves the aromatic ring, yielding 2-amino-3-carboxymuconate 6-semialdehyde, a decarboxylase forms (2Z,4E)-2-aminomuconate semialdehyde, a dehydrogenase forms (2Z,4E)-2-aminomuconate, a deaminase forms (3E)-2-oxo-3-hexenedioate (also known as 2-oxalocrotonate), and a decarboxylase forms (2Z)-2-hydroxypenta-2,4-dienoate (HPD). (lbl.gov)
Comment: Dehydrogenase praB forms 2-hydroxymuconate, tautomerase praC forms (3E)-2-oxohex-3-enedioate (2-oxalocrotonate), and decarboxylase praD yields 2-hydroxypenta-2,4-dienoate (HPD). (lbl.gov)

Comment: In MetaCyc pathway catechol degradation to HPD I (meta-cleavage, link ), dioxygenase xylE converts catechol to (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate (also known as 2-hydroxymuconate 6-semialdehyde). (lbl.gov)

Anatomy1

Organisms4

Diseases3

Chemicals and Drugs95

Analytical, Diagnostic and Therapeutic Techniques and Equipment2

Phenomena and Processes10

Information Science3

Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde. (1/2)

Purification, characterization, and sequence analysis of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas pseudoalcaligenes JS45. (2/2)

Succinate-Semialdehyde Dehydrogenase

Crotonates

Methylmalonate-Semialdehyde Dehydrogenase (Acylating)

Aminomuconate-Semialdehyde Dehydrogenase

Aldehyde Oxidoreductases

Aspartate-Semialdehyde Dehydrogenase

Aminophenols

Aminohydrolases

Brain Diseases, Metabolic, Inborn

4-Aminobutyrate Transaminase

Nitrobenzenes

Hydroxybutyrate Dehydrogenase

Sodium Oxybate

Amino Acid Metabolism, Inborn Errors

Aldehyde Dehydrogenase

Glutamate-5-Semialdehyde Dehydrogenase

Hydroxybutyrates

Succinates

Adipates

Glutarates

NAD

L-Lactate Dehydrogenase

Pseudomonas

Aspartate Kinase

Azospirillum brasilense

Decarboxylation

gamma-Aminobutyric Acid

Alcohol Dehydrogenase

NADP

Aldehydes

Molecular Sequence Data

Hydro-Lyases

Intramolecular Transferases

Glyceraldehyde-3-Phosphate Dehydrogenases

Transaminases

Amino Acid Sequence

Alcohol Oxidoreductases

Kinetics

Substrate Specificity

Acyl Coenzyme A

Glutamate Dehydrogenase

Glucosephosphate Dehydrogenase

Malate Dehydrogenase

Isocitrate Dehydrogenase

Escherichia coli

Genes, Bacterial

Cloning, Molecular

Sequence Homology, Amino Acid

Lysine

Dihydrolipoamide Dehydrogenase

Carbohydrate Dehydrogenases

2-Aminoadipic Acid

Succinate Dehydrogenase

L-Iditol 2-Dehydrogenase

Base Sequence

Glycerolphosphate Dehydrogenase

Isomerases

Homoserine Dehydrogenase

Mutation

Glucose 1-Dehydrogenase

Operon

Hydroxysteroid Dehydrogenases

Succinate-Semialdehyde Dehydrogenase (NADP+)

Bacterial Proteins

Ketoglutarate Dehydrogenase Complex

Sequence Analysis, DNA

Brain

Oxidoreductases

Saccharopine Dehydrogenases

Glucose Dehydrogenases

3-Hydroxysteroid Dehydrogenases

Phosphogluconate Dehydrogenase

Sugar Alcohol Dehydrogenases

Acyl-CoA Dehydrogenases

NADH Dehydrogenase

Malonate-Semialdehyde Dehydrogenase (Acetylating)

IMP Dehydrogenase

Lactate Dehydrogenases

Catechols

Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)