| Literature DB >> 6765200 |
H C Watson, N P Walker, P J Shaw, T N Bryant, P L Wendell, L A Fothergill, R E Perkins, S C Conroy, M J Dobson, M F Tuite.
Abstract
The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.Entities:
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Year: 1982 PMID: 6765200 PMCID: PMC553262 DOI: 10.1002/j.1460-2075.1982.tb01366.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598