From Wikipedia, the free encyclopedia
Enzyme family
Arsenate reductase (glutaredoxin) (
EC
1.20.4.1 ) is an
enzyme that
catalyzes the
chemical reaction
arsenate + glutaredoxin
⇌
{\displaystyle \rightleftharpoons }
arsenite + glutaredoxin disulfide + H2 O
Thus, the two
substrates of this enzyme are
arsenate and
glutaredoxin , whereas its 3
products are
arsenite ,
glutaredoxin disulfide , and
water .
This enzyme belongs to the family of
oxidoreductases , specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The
systematic name of this enzyme class is glutaredoxin:arsenate oxidoreductase .
Structural studies
As of late 2007, 12
structures have been solved for this class of enzymes, with
PDB accession codes
1RXE ,
1RXI ,
1S3C ,
1S3D ,
1SD8 ,
1SD9 ,
1SJZ ,
1SK0 ,
1SK1 ,
1SK2 ,
1Z2D , and
1Z2E .
References
Gladysheva T, Liu J, Rosen BP (1996).
"His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773" . J. Biol. Chem . 271 (52): 33256–60.
doi :
10.1074/jbc.271.52.33256 .
PMID
8969183 .
Gladysheva TB, Oden KL, Rosen BP (1994). "Properties of the arsenate reductase of plasmid R773". Biochemistry . 33 (23): 7288–93.
doi :
10.1021/bi00189a033 .
PMID
8003492 .
Holmgren A, Aslund F (1995). Glutaredoxin . Methods Enzymol. Vol. 252. pp. 283–92.
doi :
10.1016/0076-6879(95)52031-7 .
ISBN
978-0-12-182153-1 .
PMID
7476363 .
Silver S; Garber, Eric A. E.; Armes, L. Gene; Chen, Chih-Ming; Fuchs, James A.; Silver, Simon (1994). "Arsenate reductase of Staphylococcus aureus plasmid PI258". Biochemistry . 33 (23): 7294–7299.
doi :
10.1021/bi00189a034 .
PMID
8003493 .
Krafft T, Macy JM (1998). "Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis". Eur. J. Biochem . 255 (3): 647–53.
doi :
10.1046/j.1432-1327.1998.2550647.x .
PMID
9738904 .
Martin JL (1995).
"Thioredoxin--a fold for all reasons" . Structure . 3 (3): 245–50.
doi :
10.1016/S0969-2126(01)00154-X .
PMID
7788290 .
Messens J, Hayburn G, Desmyter A, Laus G, Wyns L (1999). "The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus". Biochemistry . 38 (51): 16857–65.
doi :
10.1021/bi9911841 .
PMID
10606519 .
Radabaugh TR, Aposhian HV (2000). "Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase". Chem. Res. Toxicol . 13 (1): 26–30.
doi :
10.1021/tx990115k .
PMID
10649963 .
Sato T, Kobayashi Y (1998).
"The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite" . J. Bacteriol . 180 (7): 1655–61.
doi :
10.1128/JB.180.7.1655-1661.1998 .
PMC
107075 .
PMID
9537360 .
Shi J, Vlamis-Gardikas A, Aslund F, Holmgren A, Rosen BP (1999).
"Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction" . J. Biol. Chem . 274 (51): 36039–42.
doi :
10.1074/jbc.274.51.36039 .
PMID
10593884 .
Activity Regulation Classification Kinetics Types