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Zenodo, 1995

DOI: 10.5281/zenodo.159789

American Society for Microbiology, Journal of Bacteriology, 19(177), p. 5561-5566, 1995

DOI: 10.1128/jb.177.19.5561-5566.1995

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Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus.

Journal article published in 1995 by Sonia Colombo, Gabriele Toietta ORCID, Laura Zecca, Marco Ercole Vanoni, Paolo Tortora
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.