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. 1982;1(12):1635–1640. doi: 10.1002/j.1460-2075.1982.tb01366.x

Sequence and structure of yeast phosphoglycerate kinase.

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, et al.
PMCID: PMC553262  PMID: 6765200

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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