Biochemistry

… and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and …

…, BW Arentson, D Srivastava, DF Becker, JJ Tanner

Index: Luo, Min; Arentson, Benjamin W.; Srivastava, Dhiraj; Becker, Donald F.; Tanner, John J. Biochemistry, 2012 , vol. 51, # 50 p. 10099 - 10108

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Citation Number: 12

Abstract

Proline dehydrogenase (PRODH) catalyzes the FAD-dependent oxidation of proline to Δ1- pyrroline-5-carboxylate, which is the first step of proline catabolism. Here, we report the structures of proline dehydrogenase from Deinococcus radiodurans in the oxidized state complexed with the proline analogue l-tetrahydrofuroic acid and in the reduced state with the proline site vacant. The analogue binds against the si face of the FAD isoalloxazine ...