1mra

From Proteopedia

Revision as of 15:36, 29 October 2007

MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE

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, with Lys 166 participating as the (S)-specific, acid/base catalyst and His 297 participating as the (R)-specific acid/base, catalyst. The dependence of kcat on pH for the racemization of both (R)-, and (S)-mandelates suggests that the pKaS of the conjugate acids of Lys, 166 and His 297 are both approximately 6.4 [Landro, J.A., Kallarakal, A.T., Ransom, S.C., Gerlt, J.A., Kozarich, J.W., Neidhart, D.J., Kenyon, G.L. (1991) ... [(full description)]

About this Structure

1MRA is a [Single protein] structure of sequence from [Pseudomonas putida] with MG and APG 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 D270N mutant., Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL, Biochemistry. 1996 May 7;35(18):5662-9. PMID:8639525

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