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Conformational preferences of the substrates of lactate dehydrogenase.

Date

Authors

Schmidt, Rebecca

Gready, Jill

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

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

URI

http://hdl.handle.net/1885/36875

Collections

ANU Research Publications

Source

Journal of Molecular Structure

Type

Journal article

DOI

10.1016/S0166-1280(99)00252-3

Restricted until

2037-12-31

Downloads

File

Description

01_Schmidt_Conformational_preferences_of_2000.pdf (352.91 KB)