Computational studies of human class V alcohol dehydrogenase - the odd sibling.

ABSTRACT:

Background

All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. This indicates that the class V ADH protein is not stable in a non-cellular environment, which is in contrast to all other human ADH enzymes. In this report we present evidence, supported with results from computational analyses performed in combination with earlier in vitro studies, why this ADH behaves in an atypical way.

Results

Using a combination of structural calculations and sequence analyses, we were able to identify local structural differences between human class V ADH and other human ADHs, including an elongated β-strands and a labile α-helix at the subunit interface region of e

SUBMITTER: Ostberg LJ 

PROVIDER: S-EPMC4960878 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature