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.
An oxidation product of tryptophan metabolism. It may be a free radical scavenger and a carcinogen.
A metabolite of tryptophan with a possible role in neurodegenerative disorders. Elevated CSF levels of quinolinic acid are correlated with the severity of neuropsychological deficits in patients who have AIDS.
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.
Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.
Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.
An NADPH-dependent flavin monooxygenase that plays a key role in the catabolism of TRYPTOPHAN by catalyzing the HYDROXYLATION of KYNURENINE to 3-hydroxykynurenine. It was formerly characterized as EC 1.14.1.2 and EC 1.99.1.5.
Benzoic acid or benzoic acid esters substituted with one or more nitro groups.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
An enzyme that catalyzes the conversion of 4-hydroxyphenylpyruvate plus oxygen to homogentisic acid and carbon dioxide. EC 1.13.11.27.
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.
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 oxidation of protocatechuate to 3-carboxy-cis-cis-muconate in the presence of molecular oxygen. It contains ferric ion. EC 1.13.11.3.
An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.
An enzyme that catalyzes the oxidation of catechol to muconic acid with the use of Fe3+ as a cofactor. This enzyme was formerly characterized as EC 1.13.1.1 and EC 1.99.2.2.
A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is a LIVER-specific enzyme that is the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.
A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE. Deficiency in the enzyme causes ALKAPTONURIA, an autosomal recessive disorder, characterized by homogentisic aciduria, OCHRONOSIS and ARTHRITIS. This enzyme was formerly characterized as EC 1.13.1.5 and EC 1.99.2.5.
A group of 1,2-benzenediols that contain the general formula R-C6H5O2.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.
  • The rate-limiting step in this pathway is the conversion of tryptophan to kynurenine by either tryptophan 2,3-dioxygenase (TDO) or indoleamine 2,3-dioxygenase 1 (IDO1). (hindawi.com)
  • The primary pathway of tryptophan metabolism, however, is the kynurenine pathway (black), by which tryptophan is converted to kynurenine via tryptophan 2,3-dioxygenase (TDO) or indoleamine 2,3-dioxygenase 1 (IDO1). (hindawi.com)
  • then, oxygenase sibC forms 3-hydroxy-L-kynurenine, which is hydrolyzed to L-alanine and 3-hydroxyanthranilate. (lbl.gov)
  • Tomić, Sanja Human 3-hydroxyanthranilate 3, 4-dioxygenase (3HAO) dynamics and reaction, a multilevel computational study. (wikipedia.org)
  • The other pathway, which results in the generation of quinolinic acid (QUIN), has multiple steps, by which kynurenine is converted to intermediates through kynurenine 3-monooxygenase (KMO) and kynureninase (KYNU) and, finally, by 3-hydroxyanthranilic acid 3,4-dioxygenase (3-HOA) to QUIN (Figure 1 ) [ 1 ]. (hindawi.com)
  • From there, it can be converted into the neuroprotective kynurenic acid (KNYA) via kynurenine aminotransferase (KAT1) or to quinolinic acid (QUIN) via a multistep process involving the enzymes kynurenine 3-monooxygenase (KMO), kynureninase (KYNU), and 3-hydroxyanthranilate 3,4-dioxygenase (3-HOA). (hindawi.com)
  • A family of alpha- KETOGLUTARIC ACID and Fe(II)-dependent dioxygenases that are homologous to AlkB, an enzyme that repairs alkylated nucleic acids in E. coli. (nih.gov)
  • A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN . (nih.gov)
  • In MetaCyc pathway anthranilate degradation IV ( link ), anthranilate hydroxylase/monooxygenase (hpaH) yields 3-hydroxyanthranilate. (lbl.gov)
  • Zhang, Y. , Colabroy, K. L. , Begley, T. P. , and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis . (anl.gov)
  • Structural and functional analysis of lignostilbene dioxygenases from Sphingobium sp. (ucdenver.edu)
  • Structure and mechanism of mouse cysteine dioxygenase. (uchicago.edu)
  • Comment: In pathway I, dioxygenase kynA opens the non-aromatic ring, to N-formyl-L-kynureine, a hydrolase yields L-kynurenine (and formate), and a hydrolase yields anthranilate and L-alanine. (lbl.gov)
  • 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)
  • For example, pathway IV yields indole-3-lactate, which could potentially be oxidized to indole-3-acetate, which has a known catabolic pathway, but no prokaryotes are known to consume tryptophan this way. (lbl.gov)
  • Pathway VIII yields tryptophol (also known as indole-3-ethanol), which could potentially be oxidized to indole-3-acetate and consumed. (lbl.gov)
  • Comment: In MetaCyc pathway anthranilate degradation I ( link ), a dioxygenase cleaves off carbon dioxide and ammonia, leaving catechol. (lbl.gov)
  • Comment: 3-hydroxyanthranilate degradation is part of L-tryptophan degradation pathway XII ( link ). (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)
  • In MetaCyc pathway catechol degradation III (ortho-cleavage, link ), the 1,2-dioxygenase catA forms cis,cis-muconate, a cycloisomerase forms (+)-muconolactone, an isomerase converts this to (4,5-dihydro-5-oxofuran-2-yl)-acetate (also known as 3-oxoadipate enol lactone), and a hydrolase cleaves this to 3-oxoadipate. (lbl.gov)
  • Comment: MetaCyc pathway 3-oxoadipate degradation ( link ) involves activation by CoA (using succinyl-CoA) and a thiolase (succinyltransferase) reaction that splits it to acetyl-CoA and succinyl-CoA. (lbl.gov)
  • In MetaCyc pathway 2-hydroxypenta-2,4-dienoate degradation ( link ), HPD is hydrated to (S)-4-hydroxy-2-oxopentanoate and an aldolase cleaves it to pyruvate and acetaldehyde. (lbl.gov)
  • PhD thesis named Computational studies of Iron dependent dioxygenases, under mentor prof. Sanja Tomić, was defended in 2014th. (wikipedia.org)
  • Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications. (uchicago.edu)
  • Zhang, Y. , White, R. H. , and Ealick, S. E. (2008) Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii . (anl.gov)
  • Comment: There are two forms of anthranilate dioxygenase, 3-subunit antABC or 4-subunit andAabcd. (lbl.gov)
  • An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways. (uchicago.edu)
  • Zhang, Y. , Colabroy, K. L. , Begley, T. P. , and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis . (anl.gov)
  • Morar, M. , White, R. H. , and Ealick, S. E. (2007) Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids . (anl.gov)
  • then, oxygenase sibC forms 3-hydroxy-L-kynurenine, which is hydrolyzed to L-alanine and 3-hydroxyanthranilate. (lbl.gov)
  • 3 HAO;3 hydroxyanthranilate 3 4 dioxygenase;3 hydroxyanthranilate dioxygenase;3 hydroxyanthranilate oxygenase;3 hydroxyanthranilic acid dioxygenase;3-HAO;3-hydroxyanthranilate 3;3-hydroxyanthranilate 3,4-dioxygenase;3-hydroxyanthranilate oxygenase;3-hydroxyanthranilic acid dioxygenase;3HAO_HUMAN;4-dioxygenase;haao;HAD;HAO. (ningbobio.com)
  • HAAO (3-hydroxyanthranilate 3,4-dioxygenase), also known as HAO or 3-HAO, is a 286 amino acid monomeric cytoplasmic protein that belongs to the 3-HAO family. (ningbobio.com)
  • Utilizing Fe2+ ions as a cofactor, HAAO participates in the formation of quinolinic acid (QUIN), and excitotoxin, by catalyzing the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (ningbobio.com)
  • use DICARBOXYLIC ACIDS 1970-1979 MH - 3-Phosphoshikimate 1-Carboxyvinyltransferase UI - D051229 MN - D8.811.913.225.735 MS - An enzyme of the shikimate pathway of AROMATIC AMINO ACID biosynthesis, it generates 5-enolpyruvylshikimate 3-phosphate and ORTHOPHOSPHATE from PHOSPHOENOLPYRUVATE and SHIKIMATE-3-PHOSPHATE. (nih.gov)
  • use AMINO ACIDS, BRANCHED-CHAIN 1979, & KETO ACIDS & VALERATES 1973-1979 MH - 3-Hydroxyanthranilate 3,4-Dioxygenase UI - D050561 MN - D8.811.682.690.416.328 MS - An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
  • Overview: Tryptophan degradation in GapMind is based on MetaCyc degradation pathways I via anthranilate ( link ), II via pyruvate ( link ), or IX via 3-hydroxyanthranilate ( link ). (lbl.gov)
  • For example, pathway IV yields indole-3-lactate, which could potentially be oxidized to indole-3-acetate, which has a known catabolic pathway, but no prokaryotes are known to consume tryptophan this way. (lbl.gov)
  • Comment: 3-hydroxyanthranilate degradation is part of L-tryptophan degradation pathway XII ( link ). (lbl.gov)
  • HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
  • HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
  • Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
  • HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)
  • An increasing evidences show that stress response was observed in cattle and goat after fed high concentrate diets exhibiting higher level of acute phase proteins including serum amyloid A (SAA) and C-reactive protein (CRP) [ 4 - 6 ]. (biomedcentral.com)
  • Comment: In MetaCyc pathway anthranilate degradation I ( link ), a dioxygenase cleaves off carbon dioxide and ammonia, leaving catechol. (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)
  • In MetaCyc pathway catechol degradation III (ortho-cleavage, link ), the 1,2-dioxygenase catA forms cis,cis-muconate, a cycloisomerase forms (+)-muconolactone, an isomerase converts this to (4,5-dihydro-5-oxofuran-2-yl)-acetate (also known as 3-oxoadipate enol lactone), and a hydrolase cleaves this to 3-oxoadipate. (lbl.gov)
  • An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
  • 9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)
  • HN - 2006(1983) MH - 2-Oxoisovalerate Dehydrogenase (Acylating) UI - D050645 MN - D8.811.682.657.350.825 MS - An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (nih.gov)
  • Pathways X and XIII yield indole-3-propionate, which may spontaneously oxidize to kynurate, but kynurate catabolism is not reported. (lbl.gov)
  • Mitochondrial liver and kidney kynurenine 3-monooxygenase activities were much higher in mouse and rat, with rabbit showing the lowest activity. (unipd.it)
  • This enzyme catalyzes the oxidative ring opening of 3-hydroxyanthranilate (1) to 2-amino-3-carboxymuconic semialdehyde (ACMS, 2) which then cyclizes to quinolinate (3). (tamu.edu)
  • 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)
  • The biosynthesis of quinolinate 3, the precursor to the pyridine ring of NAD, is still poorly understood. (tamu.edu)
  • 3-Hydroxyanthranilate 3,4-dioxygenase activity showed different behaviour in the four species. (unipd.it)
  • Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site. (umd.edu)
  • The 3-HAO family of proteins consists of intramolecular dioxygenases that contain non-heme ferrous iron. (ningbobio.com)

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