home *** CD-ROM | disk | FTP | other *** search
- *************************************************************
- * D-isomer specific 2-hydroxyacid dehydrogenases signatures *
- *************************************************************
-
- A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be
- specific for the D-isomer of their substrate have been shown [1,2,3,4] to be
- functionally and structurally related. These enzymes are listed below.
-
- - D-lactate dehydrogenase (EC 1.1.1.28), a bacterial enzyme which catalyzes
- the reduction of D-lactate to pyruvate.
- - D-glycerate dehydrogenase (EC 1.1.1.29) (NADH-dependent hydroxypyruvate
- reductase), a plant leaf peroxisomal enzyme that catalyzes the reduction of
- hydroxypyruvate to glycerate. This reaction is part of the glycolate
- pathway of photorespiration.
- - D-glycerate dehydrogenasae from the bacteria Hyphomicrobium methylovorum.
- - 3-phosphoglycerate dehydrogenase (EC 1.1.1.95), a bacterial enzyme that
- catalyzes the oxidation of D-3-phosphoglycerate to 3-phosphohydroxypyruvate.
- This reaction is the first commited step in the 'phosphorylated' pathway
- of serine biosynthesis.
- - Erythronate-4-phosphate dehydrogenase (EC 1.1.1.-) (gene pdxB), a bacterial
- enzyme involved in the biosynthesis of pyridoxine (vitamin B6).
- - D-2-hydroxyisocaproate dehydrogenase (EC 1.1.1.-) (D-hicDH), a bacterial
- enzyme that catalyzes the reversible and stereospecific interconversion
- between 2-ketocarboxylic acids and D-2-hydroxy-carboxylic acids.
- - Formate dehydrogenase (EC 1.2.1.2) (FDH) from the bacteria Pseudomonas sp.
- 101 and the yeast Hansenula polymorpha.
- - Vancomycin resistance protein vanH from Enterococcus faecium; this protein
- is a D-specific alpha-keto acid dehydrogenase involved in the formation of
- a peptidoglycan which does not terminate by D-alanine thus preventing
- vancomycin binding.
- - Emericella nidulans protein aciA.
-
- All these enzymes have similar enzymatic activities and are structurally
- related. We have selected three of the most conserved regions of these
- proteins to develop patterns. The first pattern is based on a glycine-rich
- region located in the central section of these enzymes, this region probably
- corresponds to the NAD-binding domain. The two other patterns contain a number
- of conserved charged residues, some of which may play a role in the catalytic
- mechanism.
-
- -Consensus pattern: [LIVM]-[AG]-[LIVMT]-[LIVMY]-[AG]-x-G-[NHRQS]-[LIVM]-G-
- x(13,14)-[LIVMT]-x(2)-[FYCT]-[DSTK]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [DES]-[LIVMFY](2)-x(2)-[SAC]-[DQ]-[LIVMF](2)-x-[LIVMFY]-
- [HN]-x-[PV]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: lipase 3 from Moraxella sp.
-
- -Consensus pattern: [LIVMFYA]-[KHP]-x-[GD]-x-[LIVMFYW](3)-N-x-[STAGC]-R-[GP]-
- x-[LIVM]-[LIVMC]-[DV]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for B.subtilis D-3-phosphoglycerate dehydrogenase.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Note: Escherichia coli D-lactate dehydrogenase (gene dld) does not belong to
- this family, it is a membrane-bound FAD flavoenzyme.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] Grant G.A.
- Biochem. Biophys. Res. Commun. 165:1371-1374(1989).
- [ 2] Kochhar S., Hunziker P., Leong-Morgenthaler P.M., Hottinger H.
- Biochem. Biophys. Res. Commun. 184:60-66(1992).
- [ 3] Ohta T., Taguchi H.
- J. Biol. Chem. 266:12588-12594(1991).
- [ 4] Goldberg J.D., Yoshida T., Brick P.
- J. Mol. Biol. 236:1123-1140(1994).
-