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- W937092887 abstract "Acyl-CoA dehydrogenases are flavoproteins involved in the degradation of fatty acids and of branched chain amino acids. Their reaction mechanism is assumed to involve a concerted n,s-elimination, starting with abstraction of the a-proton [1]. Incubation of medium and short chain acyl-CoA dehydrogenases (MCADH and SCADH) with 2-octynoyl-CoA leads to covalent modification of the enzyme active site [2,3]. The amino acid involved is Glu376 , which has been proposed to be the base abstracting the hydrogen as an a-proton [4]. Since Glu376 is not congerved in all acyl-CoA dehydrogenases (Isovaleryl-CoA and LCADH have Gly at position 376) [5], the above mentioned role of Glu376 can be questioned. In order to investigate the role of Glu376 , we studied the reactivity with 2-octynoyl-CoA of two enzymes lacking Glu 376 . These are long chain acyl-CoA dehydrogenase (LCADH) which has a Gly376 [5], and the Glu 376-Gln mutant of human MCADH [6].," @default.
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- W937092887 date "1991-12-31" @default.
- W937092887 modified "2023-09-24" @default.
- W937092887 title "ON THE ROLE OF GLU376 IN CATALYSIS OF ACYL-CoA DEHYDROGENASES" @default.
- W937092887 doi "https://doi.org/10.1515/9783110855425-063" @default.
- W937092887 hasPublicationYear "1991" @default.
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