S
IPR029752

D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1

InterPro entry
Short nameD-isomer_DH_CS1

Description

A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related
[1, 2, 3, 4]
. All these enzymes have similar enzymatic activities and are structurally related.

This is a glycine-rich conserved site located in the central section of these enzymes, which probably corresponds to the NAD-binding domain.

References

1.A new family of 2-hydroxyacid dehydrogenases. Grant GA. Biochem. Biophys. Res. Commun. 165, 1371-4, (1989). View articlePMID: 2692566

2.Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases. Kochhar S, Hunziker PE, Leong-Morgenthaler P, Hottinger H. Biochem. Biophys. Res. Commun. 184, 60-6, (1992). View articlePMID: 1567457

3.D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum. Taguchi H, Ohta T. J. Biol. Chem. 266, 12588-94, (1991). View articlePMID: 1840590

4.Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution. Goldberg JD, Yoshida T, Brick P. J. Mol. Biol. 236, 1123-40, (1994). View articlePMID: 8120891

Cross References

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