Conformational preferences of the substrates of lactate dehydrogenase.
Date
2000
Authors
Schmidt, Rebecca
Gready, Jill
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Abstract
The substrates of lactate dehydrogenase (pyruvate and lactate) as well as an inhibitor (oxamate) are characterized using ab initio methods employing the basis sets 6-31 +G(d) and 6-31 +G(d, p) at both RHF and MP2 levels. The first aim of these studies is
Description
Keywords
Keywords: carbon; carbonyl derivative; carboxyl group; lactate dehydrogenase; lactic acid; methyl group; oxamic acid; oxygen; pyruvic acid; accuracy; article; calculation; chemical structure; controlled study; crystal structure; energy; enthalpy; enzyme active site Ab initio; Conformer; Lactate; Lactate dehydrogenase; Oxamate; Pyruvate; Semiempirical
Citation
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Source
Journal of Molecular Structure
Type
Journal article
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2037-12-31