Molecular Cloning, Nucleotide Sequence, and Expression of a Carboxypeptidase-encoding Gene from the Archaebacterium Sulfolobus Solfataricus

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1995 Oct 1

PMID 7559343

Citations 7

Authors

S Colombo

G Toietta

L Zecca

M Vanoni

P Tortora

Affiliations

Soon will be listed here.

Abstract

Mammalian metallocarboxypeptidases play key roles in major biological processes, such as digestive-protein degradation and specific proteolytic processing. A Sulfolobus solfataricus gene (cpsA) encoding a recently described zinc carboxypeptidase with an unusually broad substrate specificity was cloned, sequenced, and expressed in Escherichia coli. Despite the lack of overall sequence homology with known carboxypeptidases, seven homology blocks, including the Zn-coordinating and catalytic residues, were identified by multiple alignment with carboxypeptidases A, B, and T. S. solfataricus carboxypeptidase expressed in E. coli was found to be enzymatically active, and both its substrate specificity and thermostability were comparable to those of the purified S. solfataricus enzyme.

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