Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity.
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.
Smulevitch
S V
SV
Institute of Microbial Genetics, Lab. of Protein Chemistry, Moscow, USSR.
Osterman
A L
AL
Galperina
O V
OV
Matz
M V
MV
Zagnitko
O P
OP
Kadyrov
R M
RM
Tsaplina
I A
IA
Grishin
N V
NV
Chestukhina
G G
GG
Stepanov
V M
VM
D000595:Amino Acid Sequence; D001483:Base Sequence; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D008848:Micromonosporaceae / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D015183:Restriction Mapping
D004269:DNA, Bacterial; D002268:Carboxypeptidases