{"title":"Molecular cloning of the Atlantic cod chymotrypsinogen B.","authors":"R Spilliaert, A Gudmundsdóttir","doi":"10.1089/10906590050145258","DOIUrl":null,"url":null,"abstract":"<p><p>The cDNA encoding Atlantic cod (Gadus morhua) chymotrypsinogen B has been isolated and sequenced. Its deduced amino acid sequence consists of a 16-residue signal sequence and a mature polypeptide of 247 residues, being two residues longer than its vertebrate analogs. This mature polypeptide corresponds to a calculated molecular mass of 26.5 kDa and shares 70% sequence identity with cod chymotrypsinogen A. However, the identity between cod chymotrypsinogen B and its other vertebrate analogues is 63-66%. In common with most fish serine proteases, cod chymotrypsinogen B contains a high number of methionine residues. The presence of a threonine instead of a highly conserved serine residue at position 189 is a novel characteristic of this enzyme. Cod chymotrypsin B, as its type B vertebrate analogs, has an alanine at position 226, whereas a glycine is most commonly found at this position in the type A chymotrypsins.</p>","PeriodicalId":79689,"journal":{"name":"Microbial & comparative genomics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/10906590050145258","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Microbial & comparative genomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1089/10906590050145258","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
The cDNA encoding Atlantic cod (Gadus morhua) chymotrypsinogen B has been isolated and sequenced. Its deduced amino acid sequence consists of a 16-residue signal sequence and a mature polypeptide of 247 residues, being two residues longer than its vertebrate analogs. This mature polypeptide corresponds to a calculated molecular mass of 26.5 kDa and shares 70% sequence identity with cod chymotrypsinogen A. However, the identity between cod chymotrypsinogen B and its other vertebrate analogues is 63-66%. In common with most fish serine proteases, cod chymotrypsinogen B contains a high number of methionine residues. The presence of a threonine instead of a highly conserved serine residue at position 189 is a novel characteristic of this enzyme. Cod chymotrypsin B, as its type B vertebrate analogs, has an alanine at position 226, whereas a glycine is most commonly found at this position in the type A chymotrypsins.