包含解淀粉芽孢杆菌α淀粉酶假定必需酪氨酸的CNBr肽的序列。

Sequence of the CNBr peptide containing the putative essential tyrosine of Bacillus amyloliquefaciens alpha amylase.

作者信息

Detera S D, Friedberg F

出版信息

Int J Pept Protein Res. 1981 Jan;17(1):93-106. doi: 10.1111/j.1399-3011.1981.tb01972.x.

DOI:10.1111/j.1399-3011.1981.tb01972.x

Abstract

The amino acid sequence of the cyanogen bromide peptide (peptide B) containing the putative essential tyrosine residue in Bacillus amyloliquefaciens alpha-amylase (EC 3.2.1.1.) was determined. It is composed of 73 amino acids and the "active" tyrosine residue is the N-terminus of the peptide. Upon iodination of the whole enzyme by means of a lactoperoxidase-catalyzed reaction, a minimum of eight tyrosine residues are iodinated. Four of these belong to peptide B. Among the cyanogen bromide peptides, B is the most readily iodinated one. Hence, it is predicted that peptide B is an exposed segment of the amylase molecule.

摘要

测定了枯草芽孢杆菌α淀粉酶（EC 3.2.1.1.）中含有假定必需酪氨酸残基的溴化氰肽（肽B）的氨基酸序列。它由73个氨基酸组成，“活性”酪氨酸残基是该肽的N端。通过乳过氧化物酶催化反应对全酶进行碘化时，至少有八个酪氨酸残基被碘化。其中四个属于肽B。在溴化氰肽中，B是最容易被碘化的一个。因此，预计肽B是淀粉酶分子的一个暴露片段。