Reference "Primary structure of carboxypeptidase III from malted barley"

Reference ID

8609

Title

Primary structure of carboxypeptidase III from malted barley

Source

Carlsberg Res Commun, 1989, vol. 54, pp. 193-202

Authors (3)

Sorensen-S-B	Svendsen-I
Breddam-K

Abstract

The primary structure of malt carboxypeptidase III has been determined. The
enzyme is a single N-terminally blocked polypeptide chain containing 411 amino
acid residues. The sequence of these amino acid residues was deduced from
analysis of fragments of the polypeptide chain obtained by chemical cleavages
with either cyanogen bromide or hydroxylamine and by enzymatic cleavages with
either trypsin, S. aureus V8 protease or proteinase A from yeast. A glycosylated
asparagine was found in position 71. The determined sequence was 97% homologous
with the amino acid sequence derived from the nucleotide sequence of a gene
coding for a wheat protein postulated to be a carboxypeptidase. The malt
carboxypeptidase III sequence showed 34% homology with the amino acid sequence
of the single-chain carboxypeptidase Y, and about 25% homology with the combined
A- and B-chains of malt carboxypeptidase I and II as well as wheat
carboxypeptidase II.