Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.20.4.1 extracted from

  • Kim, S.G.; Chung, J.S.; Sutton, R.B.; Lee, J.S.; Lopez-Maury, L.; Lee, S.Y.; Florencio, F.J.; Lin, T.; Zabet-Moghaddam, M.; Wood, M.J.; Nayak, K.; Madem, V.; Tripathy, J.N.; Kim, S.K.; Knaff, D.B.
    Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803 (2012), Biochim. Biophys. Acta, 1824, 392-403.
    View publication on PubMed
Search for more literature for 1.20.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Synechocystis sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
in silico modeling of disulfide bonds into the solution NMR structure of the fully-reduced enzyme. C8/C82 and C80C82 disulfides are equally consistent Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
C13A 114% of wild-type vmax Synechocystis sp.
C35A l00% of wild-type vmax Synechocystis sp.
C80A less than 2% of wild-type vmax Synechocystis sp.
C80A/C82A less than 2% of wild-type vmax Synechocystis sp.
C82A less than 2% of wild-type vmax Synechocystis sp.
C8A less than 2% of wild-type vmax Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0002
-
 arsenate wild-type, pH 7.5, temperature not specified in the publication Synechocystis sp.
0.0002
-
 arsenate mutant C13A, pH 7.5, temperature not specified in the publication Synechocystis sp.
0.0002
-
 arsenate mutant C35A, pH 7.5, temperature not specified in the publication Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
 x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P74313
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arsenate + reduced glutaredoxin
-
 Synechocystis sp. arsenite + oxidized glutaredoxin
-
 ?

Subunits

Subunits Comment Organism
? x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein Synechocystis sp.

Synonyms

Synonyms Comment Organism
ArsC
-
 Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
glutaredoxin replacement of the active-site Cys15 by serine completely eliminates the ability of glutatredoxin A to serve as an electron donor. Replacement of either of the two cysteine residues distant from the active site, i.e., Cys 36 and Cys70, has no effect on the electron-donating ability of glutaredoxin Synechocystis sp.