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 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.
Original language | English (US) |
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Pages (from-to) | 75-78 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 291 |
Issue number | 1 |
DOIs | |
State | Published - Oct 7 1991 |
Keywords
- Carboxypeptidase T
- Extracellular metalloenzyme
- Genomic library
- Preproenzyme
- Primary structure
- Thermoactinomyces vulgaris
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology