3-hydroxyanthranilate 3,4-dioxygenase

3-ヒドロキシアントラニル酸-3

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/25 22:57:15」(JST)

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3-hydroxyanthranilate 3,4-dioxygenase
Identifiers
EC number	1.13.11.6
CAS number	9029-50-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme that catalyzes the chemical reaction

3-hydroxyanthranilate + O₂ 2-amino-3-carboxymuconate semialdehyde

Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O₂, whereas its product is 2-amino-3-carboxymuconate semialdehyde.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3-hydroxyanthranilic acid oxidase, and 3HAO. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1YFU, 1YFW, 1YFX, 1YFY, 1ZVF, and 2QNK.

In early 2010, chemists Eli Fenyes and Jonny Skolnick were able to use the enzyme as a catalyst to synthesize stearates.

References

• DECKER RH, KANG HH, LEACH FR, HENDERSON LM (1961). "Purification and properties of 3-hydroxyanthranilic acid oxidase". J. Biol. Chem. 236: 3076–82. PMID 13884755. 
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.

UpToDate Contents

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English Journal

• An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.

• Liu F1, Geng J2, Gumpper RH3, Barman A3, Davis I2, Ozarowski A4, Hamelberg D5, Liu A6.
• The Journal of biological chemistry.J Biol Chem.2015 Jun 19;290(25):15621-34. doi: 10.1074/jbc.M115.650259. Epub 2015 Apr 27.
• The rubredoxin motif is present in over 74,000 protein sequences and 2,000 structures, but few have known functions. A secondary, non-catalytic, rubredoxin-like iron site is conserved in 3-hydroxyanthranilate 3,4-dioxygenase (HAO), from single cellular sources but not multicellular sources. Through
• PMID 25918158

• Human 3-hydroxyanthranilate 3,4-dioxygenase () dynamics and reaction, a multilevel computational study.

• Brkić H1, Kovačević B, Tomić S.
• Molecular bioSystems.Mol Biosyst.2015 Mar;11(3):898-907. doi: 10.1039/c4mb00668b. Epub 2015 Jan 15.
• 3-Hydroxyanthranilate 3,4-dioxygenase () is a non-heme iron dependent enzyme. It catalyses the cleavage of the benzene ring of 3-hydroxyanthranilic acid (3-Ohaa), an intermediate in the kynurenine pathway, and therefore represents a potential target in treating numerous disorders related to the conc
• PMID 25588817

• Vitamin B1 deficiency inhibits the increased conversion of tryptophan to nicotinamide in severe food-restricted rats.

• Shibata K1, Kobayashi R, Fukuwatari T.
• Bioscience, biotechnology, and biochemistry.Biosci Biotechnol Biochem.2015;79(1):103-8. doi: 10.1080/09168451.2014.962473. Epub 2014 Sep 25.
• The conversion of tryptophan (Trp) → nicotinamide (Nam) is an important pathway for supplying vitamin niacin. We reported the following two phenomena: (1) severe food restriction led to an increase in the Trp → Nam conversion compared with free-access control group; (2) the conversion of Trp →
• PMID 25253514

Japanese Journal

• 魚類における3-ヒドロキシアンスラニル酸オキシゲナーゼ/アミノカルボキシムコン酸セミアルデヒド脱炭酸酵素活性比からのトリプトファン-ニコチンアミド変換率の推定

• 福渡 努,真藤 こず恵,太田 万理 [他],佐々木 隆造,柴田 克己
• ビタミン 78(8), 409-411, 2004-08-25
• … In order to estimate the conversion efficiency of tryptophan-nicotinamide in freshwater fishes, carp and crucian, the liver 3-hydroxyanthranilate 3,4-dioxygenase (3-HAO) and aminocarboxymuconate-semialdehyde decarboxylase (ACMSD) activities were measured. … The activity ratios of 3-HAO/ACMSD in carp and crucian were both around 5. …
• NAID 110002843398

• Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7

• MURAKI T.
• Appl. Environ. Microbiol. 69, 1564-1572, 2003
• NAID 80015875477

• Increase in the Level of mRNA for 3-Hydroxyanthranilate 3,4-Dioxygenase in Brain of Epilepsy-prone El Mice

• , , , ,
• Bioscience, biotechnology, and biochemistry 59(11), 2191-2192, 1995-11-23
• … We had shown that production of quinolinic acid is high in the brain of epilepsy-prone El mice and that this is due to an increase in the activity of 3-hydroxyanthranilate 3,4-dioxygenase (3-HAO, EC 1.13.11.6). … We demonstrated here that the level of mRNA for 3-HAO was markedly increased in the brain of El mice. …
• NAID 110002677869

Related Links

• HAAO - 3-hydroxyanthranilate 3,4-dioxygenase - Homo ...

"Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase." Center for eukaryotic structural genomics (CESG) Submitted (JUL-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN+ ...

• 3-Hydroxyanthranilate 3,4-dioxygenase 1.1 3.11.6 - Springer

EC number 1.13.11.6 Systematic name 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing) Recommended name 3-hydroxyanthranilate 3,4-dioxygenase Synonyms 3-hydroxyanthranilate 3,4-di-3-hydroxyanthranilate ...

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★リンクテーブル★

リンク元	「3-ヒドロキシアントラニル酸-3,4-ジオキシゲナーゼ」
関連記事	「dioxygenase」

「3-ヒドロキシアントラニル酸-3,4-ジオキシゲナーゼ」

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英

3-hydroxyanthranilate 3

• 3-hydroxyanthranilate 3,4-dioxygenase

「dioxygenase」

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ジオキシゲナーゼ、二原子酸素添加酵素