BRENDA - Enzyme Database show

Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773

Liu, J.; Gladysheva, T.B.; Lee, L.; Rosen, B.P.; Biochemistry 34, 13472-13476 (1995)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.20.4.1
GSH
required
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.20.4.1
C106G
the maximal velocity is approximately half that of the wild type enzyme
Escherichia coli
1.20.4.1
C12S
catalytically inactive mutant
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.20.4.1
iodoacetate
inactivates wild type enzyme and mutant enzyme C106S, in presence of substrate, arsenate, or the competitive inhibitors phosphate or sulfate, the rate of the alkylation is reduced
Escherichia coli
1.20.4.1
NEM
-
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.20.4.1
arsenate + reduced glutaredoxin
Escherichia coli
the enzyme is involved in bacterial arsenic resistance
arsenite + oxidized glutaredoxin
-
Escherichia coli
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.20.4.1
Escherichia coli
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.20.4.1
-
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.20.4.1
arsenate + reduced glutaredoxin
C12 is located at the active site and is required for catalysis
639365
Escherichia coli
arsenite + oxidized glutaredoxin
-
-
-
-
1.20.4.1
arsenate + reduced glutaredoxin
the enzyme is involved in bacterial arsenic resistance
639365
Escherichia coli
arsenite + oxidized glutaredoxin
-
639365
Escherichia coli
?
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.20.4.1
GSH
required
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.20.4.1
C106G
the maximal velocity is approximately half that of the wild type enzyme
Escherichia coli
1.20.4.1
C12S
catalytically inactive mutant
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.20.4.1
iodoacetate
inactivates wild type enzyme and mutant enzyme C106S, in presence of substrate, arsenate, or the competitive inhibitors phosphate or sulfate, the rate of the alkylation is reduced
Escherichia coli
1.20.4.1
NEM
-
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
1.20.4.1
arsenate + reduced glutaredoxin
Escherichia coli
the enzyme is involved in bacterial arsenic resistance
arsenite + oxidized glutaredoxin
-
Escherichia coli
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.20.4.1
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.20.4.1
arsenate + reduced glutaredoxin
C12 is located at the active site and is required for catalysis
639365
Escherichia coli
arsenite + oxidized glutaredoxin
-
-
-
-
1.20.4.1
arsenate + reduced glutaredoxin
the enzyme is involved in bacterial arsenic resistance
639365
Escherichia coli
arsenite + oxidized glutaredoxin
-
639365
Escherichia coli
?