1dld

Publication Abstract from PubMed

A three-dimensional structure of the NAD-dependent D-lactate dehydrogenase of Lactobacillus bulgaricus is modeled using the structure of the formate dehydrogenase of Pseudomonas sp. as template. Both sequences share only 22% of identical residues. Regions for knowledge-based modeling are defined from the structurally conserved regions predicted by multiple alignment of a set of related protein sequences with low homology. The model of the D-LDH subunit shows, as for the formate dehydrogenase, an alpha/beta structure, with a catalytic domain and a coenzyme binding domain. It points out the catalytic histidine (His-296) and supports the hypothetical catalytic mechanism. It also suggests that the other residues involved in the active site are Arg-235, possibly involved in the binding of the carboxyl group of the pyruvate, and Phe-299, a candidate for stabilizing the methyl group of the substrate.

Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.,Vinals C, De Bolle X, Depiereux E, Feytmans E Proteins. 1995 Apr;21(4):307-18. PMID:7567953^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.