Cloned (Comment) | Organism |
---|---|
gene merA, expression as wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion proteins with a 3C protease cleavage site in Escherichia coli strain TOP10 and C43 | Shigella flexneri |
Protein Variants | Comment | Organism |
---|---|---|
C135A | site-directed mutagenesis | Shigella flexneri |
C140A | site-directed mutagenesis | Shigella flexneri |
C14A | site-directed mutagenesis | Shigella flexneri |
C561A | site-directed mutagenesis | Shigella flexneri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hg + NADP+ + H+ | Shigella flexneri | - |
Hg2+ + NADPH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Shigella flexneri | - |
gene merA from the Tn21 mer operon | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion enzymes from Escherichia coli strain C43 by amylose affinity chromatography, cleavage of the tags by 3C protease, ultrafiltration, and gel filtration | Shigella flexneri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hg + NADP+ + H+ | - |
Shigella flexneri | Hg2+ + NADPH | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | structure homology modelling, overview | Shigella flexneri |
Synonyms | Comment | Organism |
---|---|---|
MerA | - |
Shigella flexneri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | one FAD bound to each MerA catalytic core monomer | Shigella flexneri | |
NADP+ | - |
Shigella flexneri | |
NADPH | - |
Shigella flexneri |
General Information | Comment | Organism |
---|---|---|
additional information | many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that can transfer Hg2+ to the catalytic core domain (Core) for reduction to Hg0. These domains are tethered to the homodimeric core by an about 30-residue linkers that are susceptible to proteolysis, interactions of NmerA and the Core in the full-length protein, structure homology modelling amd structure-function analysis, detailed overview. Binding of Hg2+ to MerA does not alter its hydrodynamic volume | Shigella flexneri |