Structural highlights
Publication Abstract from PubMed
Hydroxyacid dehydrogenases, responsible for the stereospecific conversion of 2-keto acids to 2-hydroxyacids in lactic acid producing bacteria, have a range of biotechnology applications including antibiotic synthesis, flavor development in dairy products and the production of valuable synthons. The genome of Lactobacillus delbrueckii ssp. bulgaricus, a member of the heterogeneous group of lactic acid bacteria, encodes multiple hydroxyacid dehydrogenases whose structural and functional properties remain poorly characterized. Here, we report the apo and coenzyme NAD(+) complexed crystal structures of the L. bulgaricusD-isomer specific 2-hydroxyacid dehydrogenase, D2-HDH. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme.
Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus.,Holton SJ, Anandhakrishnan M, Geerlof A, Wilmanns M J Struct Biol. 2012 Oct 27. pii: S1047-8477(12)00291-2. doi:, 10.1016/j.jsb.2012.10.009. PMID:23110853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holton SJ, Anandhakrishnan M, Geerlof A, Wilmanns M. Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus. J Struct Biol. 2012 Oct 27. pii: S1047-8477(12)00291-2. doi:, 10.1016/j.jsb.2012.10.009. PMID:23110853 doi:http://dx.doi.org/10.1016/j.jsb.2012.10.009
