Studies of Acyl-CoA dehydrogenase catalyzed allylic isomerization: a one-base or two-base mechanism?

…, I Shin, DF Becker, MT Stankovich, H Liu

Index: Dakoji, Srikanth; Shin, Injae; Becker, Donald F.; Stankovich, Marian T.; Liu, Hung-Wen Journal of the American Chemical Society, 1996 , vol. 118, # 45 p. 10971 - 10979

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Citation Number: 22

Abstract

Acyl-CoA dehydrogenases are flavoproteins that catalyze the conversion of a fatty acyl thioester substrate to the corresponding α, β-enoyl-CoA product. It has been well established that a glutamate residue in the active site [eg, E367 in short-chain acyl-CoA dehydrogenase (SCAD) of Megasphaera elsdenii] is responsible for the initial α-proton abstraction. Early studies have also shown that this class of enzymes is capable of ...