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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.20.4.1 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.20.4.1 0.0002
-
 arsenate wild-type, pH 7.5, temperature not specified in the publication Synechocystis sp.
1.20.4.1 0.0002
-
 arsenate mutant C13A, pH 7.5, temperature not specified in the publication Synechocystis sp.
1.20.4.1 0.0002
-
 arsenate mutant C35A, pH 7.5, temperature not specified in the publication Synechocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.20.4.1 15000
-
 x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.20.4.1 Synechocystis sp. P74313
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.20.4.1 ArsC
-
 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.20.4.1 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.