5-nitrosalicylate dioxygenase

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5-nitrosalicylate dioxygenase
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EC no. 1.13.11.64
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5-nitrosalicylate dioxygenase (EC 1.13.11.64, naaB (gene)) is an enzyme with systematic name 5-nitrosalicylate:oxygen 1,2-oxidoreductase (decyclizing). [1] [2] This enzyme catalyses the following chemical reaction

5-nitrosalicylate + O2 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (overall reaction)
(1a) 5-nitrosalicylate + O2 4-nitro-6-oxohepta-2,4-dienedioate
(1b) 4-nitro-6-oxohepta-2,4-dienedioate 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (spontaneous reaction)

The enzyme from soil bacterium Bradyrhizobium sp. JS329 participates in 5-nitroanthranilate degradation.

Related Research Articles

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Catechol 2,3-dioxygenase (EC 1.13.11.2, 2,3-pyrocatechase, catechol 2,3-oxygenase, catechol oxygenase, metapyrocatechase, pyrocatechol 2,3-dioxygenase) is an enzyme with systematic name catechol:oxygen 2,3-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction

In enzymology, a 2-aminobenzenesulfonate 2,3-dioxygenase (EC 1.14.12.14) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-phenylpropanoate dioxygenase (EC 1.14.12.19) is an enzyme that catalyzes the chemical reaction

In enzymology, a biphenyl 2,3-dioxygenase (EC 1.14.12.18) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-carboxyethylcatechol 2,3-dioxygenase (EC 1.13.11.16) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-hydroxy-4-oxoquinoline 2,4-dioxygenase (EC 1.13.11.47) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Biphenyl-2,3-diol 1,2-dioxygenase</span>

Biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Protocatechuate 3,4-dioxygenase</span>

In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction

2-Hydroxymuconate-6-semialdehyde dehydrogenase (EC 1.2.1.85, xylG [gene], praB [gene] ) is an enzyme with systematic name (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

Hydroquinone 1,2-dioxygenase (EC 1.13.11.66, hydroquinone dioxygenase) is an enzyme with systematic name benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction

Carbazole 1,9a-dioxygenase (EC 1.14.12.22, CARDO) is an enzyme with systematic name 9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating). This enzyme catalyses the following chemical reaction

4-nitrocatechol 4-monooxygenase (EC 1.14.13.166) is an enzyme with systematic name 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming). This enzyme catalyses the following chemical reaction:

4-nitrophenol 4-monooxygenase (EC 1.14.13.167, pnpA (gene), pdcA (gene)) is an enzyme with systematic name 4-nitrophenol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming). This enzyme catalyses the following chemical reaction

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  1. (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + succinate
  2. (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + fumarate

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<span class="mw-page-title-main">3-Fumarylpyruvic acid</span> Chemical compound

3-Fumarylpyruvic acid, or 3-fumarylpyruvate, is a dicarboxylic acid formed from the isomerisation of 3-maleylpyruvate by maleylpyruvate isomerase. It is converted into fumarate and pyruvate by 3-fumarylpyruvate hydrolase.

References

  1. ↑ Qu Y, Spain JC (March 2010). "Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329". Applied and Environmental Microbiology. 76 (5): 1417–22. doi:10.1128/AEM.02816-09. PMC   2832354 . PMID   20081004.
  2. ↑ Qu Y, Spain JC (June 2011). "Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329". Journal of Bacteriology. 193 (12): 3057–63. doi:10.1128/JB.01188-10. PMC   3133195 . PMID   21498645.
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