Mandelate racemase: Difference between revisions
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<StructureSection load='1mdr' size='400' side='right' caption='Structure of mandelate racemase complex with reaction intermediate | <StructureSection load='1mdr' size='400' side='right' caption='Structure of mandelate racemase complex with reaction intermediate phenyl-lactate and Mg+2 ion (green) (PDB entry [[1mdr]])' scene=''> | ||
== 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>. | ||
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*Mandelate racemase binary complex | *Mandelate racemase binary complex | ||
**[[1mns]], [[1mdr]] – PpMAR + | **[[1mns]], [[1mdr]] – PpMAR + α-phenyl lactate <br /> | ||
**[[3ops]] – GeMAR + lactate<br /> | **[[3ops]] – GeMAR + lactate<br /> | ||
**[[1mra]], [[1dtn]] – PpMAR (mutant) + atrolactate<br /> | **[[1mra]], [[1dtn]] – PpMAR (mutant) + atrolactate<br /> |
Revision as of 12:58, 17 April 2016
FunctionMandelate 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[1]. Structural highlightsThe active site of MAR binds the reaction intermediate[2]. |
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3D structures of mandelate racemase3D structures of mandelate racemase
Updated on 17-April-2016
ReferencesReferences
- ↑ 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