1mdl
From Proteopedia
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MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE
Overview
On the basis of the available high-resolution structures of mandelate, racemase (MR) from Pseudomonas putida [Landro, J. A., Gerlt, J. A., Kozarich, J. W., Koo, C. W., Shah, V. J., Kenyon, G. L., Neidhart, D. J., Fujita, J., & Petsko, G. A. (1994) Biochemistry 33, 635-643], Lys 166 and, His 297 are positioned appropriately to participate in catalysis as, acid/base catalysts that either abstract the alpha-proton from the, enantiomers of mandelate to form an enolic intermediate or protonate the, enolic intermediate to form the enantiomers of mandelate, with Lys 166, participating as the (S)-specific acid/base catalyst and His 297, participating as the (R)-specific acid/base catalyst. In this paper we, report the structural and mechanistic properties of the mutant in which, Lys 166 has ... [(full description)]
About this Structure
1MDL is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with MG, RMN and SMN as [ligands]. Active as [[1]], with EC number [5.1.2.2]. Full crystallographic information is available from [OCA].
Reference
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant., Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL, Biochemistry. 1995 Mar 7;34(9):2788-97. PMID:7893690
Page seeded by OCA on Mon Oct 29 17:40:01 2007
Categories: Pseudomonas aeruginosa | Single protein | Clifton, J.G. | Petsko, G.A. | MG | RMN | SMN | Isomerase | Magnesium | Mandelate pathway
