Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Synechocystis sp. |
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 | 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 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
15000 | - |
x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | P74313 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
arsenate + reduced glutaredoxin | - |
Synechocystis sp. | arsenite + oxidized glutaredoxin | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein | Synechocystis sp. |
Synonyms | Comment | Organism |
---|---|---|
ArsC | - |
Synechocystis sp. |
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. |