Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity

FEBS Lett. 1991 Oct 7;291(1):75-8. doi: 10.1016/0014-5793(91)81107-j.

Abstract

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 of 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.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Carboxypeptidases / genetics*
  • Carboxypeptidases / metabolism
  • Cloning, Molecular
  • DNA, Bacterial
  • Micromonosporaceae / enzymology
  • Micromonosporaceae / genetics*
  • Molecular Sequence Data
  • Restriction Mapping

Substances

  • DNA, Bacterial
  • Carboxypeptidases

Associated data

  • GENBANK/S60778
  • GENBANK/S62628
  • GENBANK/S62632
  • GENBANK/S62637
  • GENBANK/S62640
  • GENBANK/S62644
  • GENBANK/S62648
  • GENBANK/S62652
  • GENBANK/X56901
  • GENBANK/X58803