Article
The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants.
Biochemistry - 13 Jul 2004
Gattis James L, Ruben Eliza, Fenley Marcia O, Ellington W Ross, Chapman Michael S
Abstract excerpt
Arginine kinase buffers cellular ATP levels by catalyzing reversible phosphoryl transfer between ATP and arginine. A conserved cysteine has long been thought important in catalysis. Here, cysteine 271 of horseshoe crab arginine kinase has been mutated to serine, alanine, asparagine, or aspartate. Catalytic turnover rates were 0.02-1.0% of wild type, but the activity of uncharged mutations could be partially...
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