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Information on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin) and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.20.4.1
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IUBMB Comments
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
arsenate
+
glutathione
+
glutaredoxin
=
arsenite
+
a glutaredoxin-glutathione disulfide
+
H2O
+
+
=
+
a glutaredoxin-glutathione disulfide
+
Synonyms
arsenate reductase, asv reductase, acr2p, pvgrx5, slr0946, synarsc, all0195, pcacr2, mxan_0575, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acr2p
-
-
-
-
ArsC
-
-
-
-
arsenate reductase (glutaredoxin)
-
-
-
-
gene arsC proteins
-
-
-
-
glutathione:arsenate oxidoreductase
-
-
-
-
proteins (specific proteins and subclasses), gene arsC
-
-
-
-
reductase, arsenate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arsenate:glutathione/glutaredoxin oxidoreductase
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
146907-46-2
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A2R3J0T9_PSEAI
117
0
12780
TrEMBL
-
A0A0F6RRY1_PSEAI
140
0
15463
TrEMBL
-
A0A485HFC6_PSEAI
117
0
12764
TrEMBL
-
A0A8G4CBC2_PSEAI
276
0
29870
TrEMBL
-
A0A8G6A7V7_PSEAI
140
0
15529
TrEMBL
-
B3G202_PSEAI
140
0
15439
TrEMBL
-
A0A8G2UVN2_PSEAI
117
0
12762
TrEMBL
-
A0A3S3TA88_PSEAI
117
0
12762
TrEMBL
-
A0A8G5H206_PSEAI
117
0
12762
TrEMBL
-
A0A6A9K169_PSEAI
117
0
12818
TrEMBL
-
A0A8G7FDW8_PSEAI
140
0
15445
TrEMBL
-
A0A431X9E1_PSEAI
117
0
12750
TrEMBL
-
A0A0C7ACK7_PSEAI
117
0
12790
TrEMBL
-
A0A844NIL8_PSEAI
140
0
15379
TrEMBL
-
A0A8G6V2Y8_PSEAI
117
0
12815
TrEMBL
-
A0A8G2VLF0_PSEAI
117
0
12804
TrEMBL
-
A0A8G6FX82_PSEAI
117
0
12774
TrEMBL
-
A0A0A8RSZ7_PSEAI
140
0
15467
TrEMBL
-
A0A4V8DU71_PSEAI
117
0
12777
TrEMBL
-
A0A2C9WZ80_PSEAI
117
0
12804
TrEMBL
-
A0A8G7FJ34_PSEAI
140
0
15366
TrEMBL
-
A0A5E5QZT2_PSEAI
117
0
12776
TrEMBL
-
A0A0A8RJ18_PSEAI
117
0
12691
TrEMBL
-
A0A231IFV0_PSEAI
140
0
15641
TrEMBL
-
A0A5M6GUL0_PSEAI
117
0
12818
TrEMBL
-
A0A485EYI1_PSEAI
140
0
15621
TrEMBL
-
A0A8G3NB18_PSEAI
140
0
15339
TrEMBL
-
A0A8G6QW39_PSEAI
140
0
15454
TrEMBL
-
A0A8F9PJR8_PSEAI
140
0
15337
TrEMBL
-