Mandelate racemase: Difference between revisions
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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 | '''Mandelate racemase''' (MAR) catalyzes the interconversion of enantiomers of mandelate [[R/S nomenclature|(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>. | ||
== Structural highlights == | == Structural highlights == | ||
The active site of MAR binds the reaction intermediate<ref>PMID:8292591</ref>. | The biological assembly of mandelate racemase from ''Pseudomonas putida'' is <scene name='51/516478/Cv/7'>homooctamer</scene>. The <scene name='51/516478/Cv/8'>active site of MAR binds the reaction intermediate</scene><ref>PMID:8292591</ref>. Water molecule are shown as red sphere. | ||
</StructureSection> | </StructureSection> | ||
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*Mandelate racemase binary complex | *Mandelate racemase binary complex | ||
**[[1mns]], [[1mdr]] – PpMAR + | **[[1mns]], [[1mdr]] – PpMAR + α-phenyl lactate <br /> | ||
**[[1mra]], [[1dtn]] – PpMAR (mutant) + atrolactate<br /> | **[[1mra]], [[1dtn]] – PpMAR (mutant) + atrolactate<br /> | ||
**[[1mdl]] - PpMAR (mutant) + mandelate<br /> | **[[1mdl]] - PpMAR (mutant) + mandelate<br /> | ||
| Line 50: | Line 49: | ||
**[[4m6u]] - PpMAR + tartronic acid<br /> | **[[4m6u]] - PpMAR + tartronic acid<br /> | ||
**[[4fp1]] – PpMAR + inhibitor<br /> | **[[4fp1]] – PpMAR + inhibitor<br /> | ||
**[[ | **[[4x2p]] – PpMAR + 3-hydroxypyruvate<br /> | ||
**[[6vim]], [[7mqx]] – PpMAR + boronic acid derivative<br /> | |||
**[[3uxk]], [[3uxl]] – PpMAR + intermediate analog<br /> | **[[3uxk]], [[3uxl]] – PpMAR + intermediate analog<br /> | ||
**[[3sbf]] – VbMAR (mutant) + arabinonate <br /> | **[[3sbf]] – VbMAR (mutant) + arabinonate <br /> | ||
| Line 56: | Line 56: | ||
**[[4gfi]] – AtMAR + dipeptide epimerase<br /> | **[[4gfi]] – AtMAR + dipeptide epimerase<br /> | ||
**[[4h19]] – AtMAR + ribonohydroxamate<br /> | **[[4h19]] – AtMAR + ribonohydroxamate<br /> | ||
**[[3ops]] – GeMAR + lactate<br /> | |||
**[[3tte]] - BrMAR + mandelate<br /> | |||
}} | }} | ||
== References == | == References == | ||
Latest revision as of 09:52, 28 October 2021
FunctionMandelate racemase (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 biological assembly of mandelate racemase from Pseudomonas putida is . The [2]. Water molecule are shown as red sphere. |
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3D structures of mandelate racemase3D structures of mandelate racemase
Updated on 28-October-2021
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