IVD Protein, Human (sf9, His)

IVD is a key enzyme responsible for catalyzing the conversion of isovaleryl-CoA/3-methylbutyryl-CoA into 3-methylbut-2-enoyl-CoA, which is an important intermediate step in the leucine catabolism pathway. . This enzyme activity is essential for the breakdown of the branched-chain amino acid leucine and contributes to the regulation of metabolic processes. IVD Protein, Human (sf9, His) is the recombinant human-derived IVD protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of IVD Protein, Human (sf9, His) is 394 a.a., with molecular weight of ~43 kDa.

Isovaleryl-CoA dehydrogenase (IVD) is a crucial enzyme in the leucine catabolic pathway, catalyzing the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA. This enzymatic step is a key intermediate in the breakdown of leucine. In addition to its primary role in leucine metabolism, IVD exhibits the ability to oxidize other saturated short-chain acyl-CoA thioesters, including pentanoyl-CoA, hexenoyl-CoA, and butenoyl-CoA, albeit to a lesser extent. These broader substrate capabilities suggest that IVD may contribute to the oxidation of various short-chain fatty acids, expanding its metabolic role beyond leucine catabolism. The multifunctional nature of IVD underscores its importance in maintaining metabolic homeostasis by participating in the degradation of diverse acyl-CoA substrates (adapted from the provided passage).

Human

Sf9 insect cells

N-His

P26440-1 (H33-H426)

3712  [NCBI]

Approximately 43 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.