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D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase.

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Bernard, N. Johnsen, K Holbrook, J J Delcour, Jean [UCL]

The NAD-dependent D-(-)-lactate dehydrogenase (D-LDH) from Lactobacillus delbrueckii subsp. bulgaricus (in short, L. bulgaricus) has been modified at position 175 by site-directed mutagenesis, changing a conserved aspartate residue into an alanine. The D175A mutant enzyme displays a 40-fold shift in coenzyme preference from NADH to NADPH. This demonstrates that D175 truly belongs to the amino acid consensus GXGXXGX(17)D (where X represents any residue) which is the signature of the coenzyme binding site of most NAD-dependent dehydrogenases.

Document type Article de périodique (Journal article) – Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
Access type Accès restreint
Publication date 1995
Journal information "Biochemical and biophysical research communications" - Vol. 208, no. 3, p. 895-900 (1995)
Peer reviewed yes
issn 0006-291X
Publication status Publié
Affiliation UCL - SC/BIOL - Département de biologie
MESH Subject Alanine ; Amino Acid Sequence ; Aspartic Acid ; Bacteria - enzymology ; Base Sequence ; Binding Sites ; Consensus Sequence ; Kinetics ; L-Lactate Dehydrogenase - chemistry - isolation & purification - metabolism ; Lactobacillus - enzymology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; NAD - metabolism ; NADP - metabolism ; Oligodeoxyribonucleotides ; Point Mutation ; Recombinant Proteins - chemistry - isolation & purification - metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
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Bibliographic reference Bernard, N. ; Johnsen, K ; Holbrook, J J ; Delcour, Jean. D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase.. In: Biochemical and biophysical research communications, Vol. 208, no. 3, p. 895-900 (1995)
Permanent URL http://hdl.handle.net/2078.1/11891