BRENDA - Enzyme Database
show all sequences of 1.2.99.7

Nitrite reduction by xanthine oxidase family enzymes: a new class of nitrite reductases

Maia, L.B.; Moura, J.J.; J. Biol. Inorg. Chem. 16, 443-460 (2011)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Desulfovibrio gigas
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
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Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Desulfovibrio gigas
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Purification (Commentary)
Commentary
Organism
-
Desulfovibrio gigas
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
benzaldehyde + H2O + oxidized 2,6-dichlorophenolindophenol
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725548
Desulfovibrio gigas
benzoate + reduced 2,6-dichlorophenol-indophenol
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?
additional information
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
725548
Desulfovibrio gigas
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Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme contains no FAD
Desulfovibrio gigas
[2Fe-2S]-center
the enzyme contains two [2Fe–2S] centers
Desulfovibrio gigas
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme contains no FAD
Desulfovibrio gigas
[2Fe-2S]-center
the enzyme contains two [2Fe–2S] centers
Desulfovibrio gigas
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Desulfovibrio gigas
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
?
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Purification (Commentary) (protein specific)
Commentary
Organism
-
Desulfovibrio gigas
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
benzaldehyde + H2O + oxidized 2,6-dichlorophenolindophenol
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725548
Desulfovibrio gigas
benzoate + reduced 2,6-dichlorophenol-indophenol
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-
?
additional information
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
725548
Desulfovibrio gigas
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Other publictions for EC 1.2.99.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740765
Correia
Aromatic aldehydes at the acti ...
Desulfovibrio gigas
J. Biol. Inorg. Chem.
20
219-229
2015
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Gomez
Isotropic exchange interaction ...
Desulfovibrio gigas
J. Biol. Inorg. Chem.
20
233-242
2015
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741287
Marangon
Kinetic and structural studies ...
Desulfovibrio gigas
PLoS ONE
8
e83234
2013
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725548
Maia
Nitrite reduction by xanthine ...
Desulfovibrio gigas
J. Biol. Inorg. Chem.
16
443-460
2011
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712240
Santos-Silva
Kinetic, structural, and EPR s ...
Desulfovibrio gigas
J. Am. Chem. Soc.
131
7990-7998
2009
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655476
Correia dos Santos
Direct electrochemistry of the ...
Desulfovibrio gigas
Eur. J. Biochem.
271
1329-1338
2004
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644705
Uchida
Purification and characterizat ...
Pseudomonas sp., Pseudomonas sp. KY 469
FEMS Microbiol. Lett.
229
31-36
2003
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656294
Rebelo
Structure refinement of the al ...
Desulfovibrio gigas
J. Biol. Inorg. Chem.
6
791-800
2001
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644707
Andrade
Aldehyde oxidoreductase activi ...
Desulfovibrio alaskensis, Desulfovibrio alaskensis NCIMB 1349, Desulfovibrio alaskensis NCIMB 13491
Eur. J. Biochem.
267
2054-2061
2000
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654573
Caldeira
Analysis of the electron param ...
Desulfovibrio gigas
Biochemistry
39
2700-2707
2000
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657173
Huber
A structure-based catalytic me ...
Desulfovibrio gigas
Proc. Natl. Acad. Sci. USA
93
8846-8851
1996
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11936
Hensgens
Purification and characterizat ...
Desulfovibrio gigas
J. Bacteriol.
177
6195-6200
1995
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655399
Thoenes
Molecular cloning and sequence ...
Desulfovibrio gigas
Eur. J. Biochem.
220
901-910
1994
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654563
Barata
Aldehyde oxidoreductase activi ...
Desulfovibrio gigas
Biochemistry
32
11559-11568
1993
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655397
Romao
Subunit composition, crystalli ...
Desulfovibrio gigas
Eur. J. Biochem.
215
729-732
1993
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654473
Bray
Information from EPR spectrosc ...
Desulfovibrio gigas
Biochem. J.
280
817-820
1991
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390386
Turner
The molybdenum iron-sulphur pr ...
Desulfovibrio gigas
Biochem. J.
243
755-761
1987
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