Noncanonical interactions between serpin and β-amylase in barley grain improve β-amylase activity in vitro.

ABSTRACT: Serpin protease inhibitors and β-amylase starch hydrolases are very abundant seed proteins in the endosperm of grasses. β-amylase is a crucial enzyme in the beer industry providing maltose for fermenting yeast. In animals and plants, inhibitory serpins form covalent linkages that inactivate their cognate proteases. Additionally, in animals, noninhibitory functions for serpins are observed such as metabolite carriers and chaperones. The function of serpins in seeds has yet to be unveiled. In developing endosperm, serpin Z4 and β-amylase showed similar in vivo spatio-temporal accumulation properties and colocalize in the cytosol of transformed tobacco leaves. A molecular interaction between recombinant proteins of serpin Z4 and β-amylase was revealed by surface plasmon resonance and m

SUBMITTER: Cohen M 

PROVIDER: S-EPMC6508567 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature