Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.

doi:10.1006/mgme.2001.3234

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Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.

Molecular genetics and metabolism - 1 Jan 2000

Volchenboum S L, Mohsen A W, Kim J J, Vockley J

Abstract excerpt

Isovaleryl-CoA dehydrogenase (IVD) is a homotetrameric flavoenzyme, which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA and transfers electrons to the electron-transferring flavoprotein, and is a member of the acyl-CoA dehydrogenase (ACD) enzyme family. Human IVD crystal structure with a bound substrate analogue shows the guanidino group of Arg387, a conserved residue among other members of...

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Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.

Abstract excerpt

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Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.

Abstract excerpt

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