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Primary structure of carboxypeptidase ii from malted barley

Primary structure of carboxypeptidase ii from malted barley

Carlsberg Research Communications 52(4): 285-296

The primary structure of malt carboxypeptidase II has been determined. The enzyme is a dimer where each monomer is composed of two peptide chains, an A- and a B-chain, linked by disulphide bridges. The B-chain exists in two forms, both N-terminally blocked, which differ in position 38 and 39, one form containing Ala38-Thr39, the other containing Thr38-Asn39 with carbohydrate attached to the asparagine side-chain. Fragments of the A- and B-chains were obtained by chemical cleavages with either cyanogen bromide, hydroxylamine or iodosobenzoic acid and by enzymatic cleavages with either trypsin or S. aureus V8 protease, sequenced and aligned to give the total sequence. The A- and B-chains contain 260 and 159 amino acid residues, respectively. Glycosylated asparagines are found in positions 114, 125 and 257 of the A-chain, and positions 28, 34, 39 and 159 of the B-chain. Position 39 of the B-chain is only partially glycosylated (see above). Alignment of the sequence of the A-chain with the N-terminal part of carboxypeptidase Y revealed 28% homology. Similarly, the B-chain showed 21% homology with the C-terminal part of carboxypeptidase Y. The homology between malt carboxypeptidases I and II is 40% for the A-chains and 30% for the B-chains. The corresponding homologies between malt carboxypeptidase II and wheat carboxypeptidase II are 95% and 96%, respectively. No homology was observed with other proteins by a computer search of a sequence data base provided by the National Biomedical Research Foundation. A region of the A-chain was identical to the region around the essential seryl residue in position 146 of carboxypeptidase Y.

Accession: 006184834

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DOI: 10.1007/bf02907171

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