Mandelate racemase
From Proteopedia
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| - | <StructureSection load='1mdr' size=' | + | <StructureSection load='1mdr' size='350' side='right' caption='Structure of mandelate racemase complex with reaction intermediate phenyl-lactate and Mg+2 ion (green) (PDB entry [[1mdr]])' scene='51/516478/Cv/1'> |
== Function == | == Function == | ||
'''Mandelate rasemase''' (MAR) catalyzes the interconversion of enantiomers of mandelate (S to R). MAR is Mg-dependent. MAR can racemize other alpha-hydroxy carbonyl compounds. MAR is involved in aromatic acids catabolism<ref>PMID:1892833</ref>. | '''Mandelate rasemase''' (MAR) catalyzes the interconversion of enantiomers of mandelate (S to R). MAR is Mg-dependent. MAR can racemize other alpha-hydroxy carbonyl compounds. MAR is involved in aromatic acids catabolism<ref>PMID:1892833</ref>. | ||
Revision as of 10:21, 2 August 2018
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3D structures of mandelate racemase
Updated on 02-August-2018
References
- ↑ Powers VM, Koo CW, Kenyon GL, Gerlt JA, Kozarich JW. Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism. Biochemistry. 1991 Sep 24;30(38):9255-63. PMID:1892833
- ↑ Landro JA, Gerlt JA, Kozarich JW, Koo CW, Shah VJ, Kenyon GL, Neidhart DJ, Fujita S, Petsko GA. The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate. Biochemistry. 1994 Jan 25;33(3):635-43. PMID:8292591
