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Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T A metalloenzyme endowed with dual substrate specificity
Author(s) -
Smulevitch Sergey V.,
Osterman Andrey L.,
Galperina Olga V.,
Matz Mikhail V.,
Zagnitko Olga P.,
Kadyrov Rafail M.,
Tsaplina Iraida A.,
Grishin Nikolai V.,
Chestukhina Galina G.,
Stepanov Valentin M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81107-j
Subject(s) - carboxypeptidase , biochemistry , carboxypeptidase a , enzyme , protein primary structure , active site , chemistry , amino acid , cloning (programming) , biology , gene , peptide sequence , stereochemistry , computer science , programming language
A gene coding for an extracellular Zn‐carboxypeptidase of Thermoactinomyces vulgaris has been cloned and sequenced (EMBL X56901). This enzyme named carboxypeptidase T reveals simultaneously both types of substrate specificity characteristic of mammalian carboxypeptidases A and B. The carboxypeptidase T gene is primarily expressed in E. coli as a non‐active preproenzyme with an additional 98 amino acid residues at the N‐terminus. Primary structure alignment or mature carboxypeptidase T and mammalian metallocarboxypeptidases demonstrated 25–30% overall identity but a full preservation of presumed catalytically important residues. These observations imply a basic uniformity of the general catalytic mechanism for enzymes of that class produced by evolutionarily remote organisms.