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Literature summary for 1.20.4.1 extracted from

  • Gladysheva, T.B.; Oden, K.L.; Rosen, B.P.
    Properties of the arsenate reductase of plasmid R773 (1994), Biochemistry, 33, 7288-7293.
    View publication on PubMed
Search for more literature for 1.20.4.1

Activating Compound

Activating Compound Comment Organism Structure
GSH glutathione is not effective as electron donor Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
arsenite
-
 Escherichia coli
NEM
-
 Escherichia coli
phosphate poor Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8
-
 arsenate
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arsenate + reduced glutaredoxin Escherichia coli the enzyme is involved in bacterial arsenic resistance arsenite + oxidized glutaredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arsenate + reduced glutaredoxin strong specificity for arsenate Escherichia coli arsenite + oxidized glutaredoxin
-
 ?
arsenate + reduced glutaredoxin thioredoxin is not effective as electron donor Escherichia coli arsenite + oxidized glutaredoxin
-
 ?
arsenate + reduced glutaredoxin the enzyme is involved in bacterial arsenic resistance Escherichia coli arsenite + oxidized glutaredoxin
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 reductase activity increases from 10°C to 40°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3 6.8
-
 Escherichia coli