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Mandelate dehydrogenase

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<StructureSection load='2a7p' size='400' side='right' caption='Structure of monomer of S-mandelate dehydrogenase tetramer complex with 3-indolelactate and flavin mononucleotide (PDB entry [[2a7p]])' scene=''>
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<StructureSection load='2a7p' size='450' side='right' caption='Structure of monomer of S-mandelate dehydrogenase tetramer complex with 3-indolelactate and flavin mononucleotide (PDB entry [[2a7p]])' scene=''>
== Function ==
== Function ==
'''S-mandelate dehydrogenase''' (SMD) catalyzes the conversion of S-2-hydroxy-2-phenylacetate and acceptor to 2-oxo-2-phenylacetate and reduced acceptor<ref>PMID:10231535</ref>. SMD is a FMN-dependent enzyme. '''D-mandelate dehydrogenase''' (DMD) catalyzes the NAD-dependent oxidation of D-mandalate to phenylglyoxylate.
'''S-mandelate dehydrogenase''' (SMD) catalyzes the conversion of S-2-hydroxy-2-phenylacetate and acceptor to 2-oxo-2-phenylacetate and reduced acceptor<ref>PMID:10231535</ref>. SMD is a FMN-dependent enzyme. '''D-mandelate dehydrogenase''' (DMD) catalyzes the NAD-dependent oxidation of D-mandalate to phenylglyoxylate.

Revision as of 13:00, 19 April 2016

Structure of monomer of S-mandelate dehydrogenase tetramer complex with 3-indolelactate and flavin mononucleotide (PDB entry 2a7p)

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3D structures of mandelate dehydrogenase

Updated on 19-April-2016

References

  1. ↑ 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:http://dx.doi.org/10.1021/bi990024m
  2. ↑ 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

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Michal Harel, Alexander Berchansky

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