BRENDA - Enzyme Database show

Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow

Siegel, L.M.; Davis, P.S.; Kamin, H.; J. Biol. Chem. 249, 1572-1586 (1974)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.8.1.2
arsenite
-
Escherichia coli
1.8.1.2
Br-
-
Escherichia coli
1.8.1.2
Cl-
-
Escherichia coli
1.8.1.2
CN-
-
Escherichia coli
1.8.1.2
CO
-
Escherichia coli
1.8.1.2
F-
-
Escherichia coli
1.8.1.2
NADP+
NADPH-dependent activities
Escherichia coli
1.8.1.2
NO3-
-
Escherichia coli
1.8.1.2
p-Mercuriphenylsulfonate
-
Escherichia coli
1.8.1.2
SCN-
-
Escherichia coli
1.8.1.2
sulfate
-
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.1.2
0.0043
0.0074
sulfite
-
Escherichia coli
1.8.1.2
0.8
1.5
nitrite
-
Escherichia coli
1.8.1.2
4.5
10.5
hydroxylamine
-
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.8.1.2
sulfite + NADPH + H+
Escherichia coli
no physiological nitrite reductase
sulfide + NADP+ + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.1.2
Escherichia coli
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
1.8.1.2
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
mechanism of electron transfer
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.1.2
hydroxylamine + NADPH
NADPH can be replaced by reduced methyl viologen
392964
Escherichia coli
ammonia + NADP+
-
392964
Escherichia coli
?
1.8.1.2
additional information
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
392964
Escherichia coli
?
-
-
-
-
1.8.1.2
additional information
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
392964
Escherichia coli
?
-
-
-
-
1.8.1.2
NADP+ + reduced methyl viologen
-
392964
Escherichia coli
NADPH + oxidized methyl viologen
-
-
-
?
1.8.1.2
nitrite + NADPH
-
392964
Escherichia coli
ammonia + NADP+
-
392964
Escherichia coli
?
1.8.1.2
sulfite + NADPH
NADPH can be replaced by reduced methyl viologen
392964
Escherichia coli
sulfide + NADP+ + H2O
-
392964
Escherichia coli
?
1.8.1.2
sulfite + NADPH + H+
no physiological nitrite reductase
392964
Escherichia coli
sulfide + NADP+ + H2O
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8.1.2
1.25
-
NADPH
cosubstrate O2
Escherichia coli
1.8.1.2
30
40
sulfite
cosubstrate NADPH
Escherichia coli
1.8.1.2
43.3
51.7
nitrite
cosubstrate NADPH
Escherichia coli
1.8.1.2
65
-
sulfite
cosubstrate reduced methyl viologen
Escherichia coli
1.8.1.2
98.3
217
hydroxylamine
cosubstrate NADPH
Escherichia coli
1.8.1.2
158
-
NADPH
cosubstrate 3-acetylpyridineadenine dinucleotide phosphate
Escherichia coli
1.8.1.2
172
-
NADPH
cosubstrate FMN
Escherichia coli
1.8.1.2
318
-
NADPH
cosubstrate cytochrome c
Escherichia coli
1.8.1.2
462
-
NADPH
cosubstrate dichlorphenolindophenol
Escherichia coli
1.8.1.2
468
-
NADPH
cosubstrate ferricyanide
Escherichia coli
1.8.1.2
605
-
NADP+
-
Escherichia coli
1.8.1.2
605
-
reduced methyl viologen
-
Escherichia coli
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.8.1.2
7.9
-
sulfite
Escherichia coli
1.8.1.2
8.6
-
nitrite
Escherichia coli
1.8.1.2
9.5
-
hydroxylamine
Escherichia coli
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.8.1.2
flavin
treatment with p-chloromercuriphenylsulfonate causes dissociation of FMN but retetion of FAD and heme
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.8.1.2
flavin
treatment with p-chloromercuriphenylsulfonate causes dissociation of FMN but retetion of FAD and heme
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.8.1.2
arsenite
-
Escherichia coli
1.8.1.2
Br-
-
Escherichia coli
1.8.1.2
Cl-
-
Escherichia coli
1.8.1.2
CN-
-
Escherichia coli
1.8.1.2
CO
-
Escherichia coli
1.8.1.2
F-
-
Escherichia coli
1.8.1.2
NADP+
NADPH-dependent activities
Escherichia coli
1.8.1.2
NO3-
-
Escherichia coli
1.8.1.2
p-Mercuriphenylsulfonate
-
Escherichia coli
1.8.1.2
SCN-
-
Escherichia coli
1.8.1.2
sulfate
-
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.1.2
0.0043
0.0074
sulfite
-
Escherichia coli
1.8.1.2
0.8
1.5
nitrite
-
Escherichia coli
1.8.1.2
4.5
10.5
hydroxylamine
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.8.1.2
sulfite + NADPH + H+
Escherichia coli
no physiological nitrite reductase
sulfide + NADP+ + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.1.2
hydroxylamine + NADPH
NADPH can be replaced by reduced methyl viologen
392964
Escherichia coli
ammonia + NADP+
-
392964
Escherichia coli
?
1.8.1.2
additional information
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
392964
Escherichia coli
?
-
-
-
-
1.8.1.2
additional information
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
392964
Escherichia coli
?
-
-
-
-
1.8.1.2
NADP+ + reduced methyl viologen
-
392964
Escherichia coli
NADPH + oxidized methyl viologen
-
-
-
?
1.8.1.2
nitrite + NADPH
-
392964
Escherichia coli
ammonia + NADP+
-
392964
Escherichia coli
?
1.8.1.2
sulfite + NADPH
NADPH can be replaced by reduced methyl viologen
392964
Escherichia coli
sulfide + NADP+ + H2O
-
392964
Escherichia coli
?
1.8.1.2
sulfite + NADPH + H+
no physiological nitrite reductase
392964
Escherichia coli
sulfide + NADP+ + H2O
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8.1.2
1.25
-
NADPH
cosubstrate O2
Escherichia coli
1.8.1.2
30
40
sulfite
cosubstrate NADPH
Escherichia coli
1.8.1.2
43.3
51.7
nitrite
cosubstrate NADPH
Escherichia coli
1.8.1.2
65
-
sulfite
cosubstrate reduced methyl viologen
Escherichia coli
1.8.1.2
98.3
217
hydroxylamine
cosubstrate NADPH
Escherichia coli
1.8.1.2
158
-
NADPH
cosubstrate 3-acetylpyridineadenine dinucleotide phosphate
Escherichia coli
1.8.1.2
172
-
NADPH
cosubstrate FMN
Escherichia coli
1.8.1.2
318
-
NADPH
cosubstrate cytochrome c
Escherichia coli
1.8.1.2
462
-
NADPH
cosubstrate dichlorphenolindophenol
Escherichia coli
1.8.1.2
468
-
NADPH
cosubstrate ferricyanide
Escherichia coli
1.8.1.2
605
-
NADP+
-
Escherichia coli
1.8.1.2
605
-
reduced methyl viologen
-
Escherichia coli
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.8.1.2
7.9
-
sulfite
Escherichia coli
1.8.1.2
8.6
-
nitrite
Escherichia coli
1.8.1.2
9.5
-
hydroxylamine
Escherichia coli