| Function
S-mandelate dehydrogenase (SMD) catalyzes the conversion of S-2-hydroxy-2-phenylacetate and acceptor to 2-oxo-2-phenylacetate and reduced acceptor[1]. SMD is a FMN-dependent enzyme. D-mandelate dehydrogenase (DMD) catalyzes the NAD-dependent oxidation of D-mandalate to phenylglyoxylate.
Structural highlights
The biological assembly of SMD from Pseudomonas putida is homotetramer. The poor substrate indolelactate binds in the active site of SMD[2]. Water molecules shown as red spheres.
- ↑ Lehoux IE, Mitra B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects. Biochemistry. 1999 May 4;38(18):5836-48. PMID:10231535 doi:https://dx.doi.org/10.1021/bi990024m
- ↑ Sukumar N, Dewanti A, Merli A, Rossi GL, Mitra B, Mathews FS. Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):543-52. Epub 2009, May 15. PMID:19465768 doi:10.1107/S0907444909010270
|
3D structures of mandelate dehydrogenase
Updated on 14-December-2025
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- S-mandelate dehydrogenase
- 6bfg – PpSM + FMN - Pseudomonas putida
- 1huv, 1p4c, 1p5b, 2a7n, 3giy – PpSM (mutant) + FMN
- 2a7p – PpSMD (mutant) + FMN + 3-indolelacetate
- 2a85 – PpSMD (mutant) + FMN + 2-hydroxyoctanoate
- 8wl1 – LbSMD – Levilactobacillus brevis
- 8wl3, 8wl4 – LbSMD (mutant)
- D-mandelate dehydrogenase
- 2w2k – RgDMD – Rhodotorula graminis
- 2w2l – RgDMD + NAD
- 3wfi – EfDMD – Enterococcus faecium
- 3wfj – EfDMD + NAD
- 5x20 – EfDMD + NAD + aniline(oxo)acetate
References
