Carboxypeptidase T Explained
Carboxypeptidase T |
Ec Number: | 3.4.17.18 |
Cas Number: | 89623-65-4 |
Carboxypeptidase T (CPT) is a hydrolytic enzyme.[1] [2] [3] This enzyme catalyses the following chemical reaction:
Releases a C-terminal residue, which may be hydrophobic or positively charged.
This enzyme is isolated from Thermoactinomyces vulgaris.
Notes and References
- Osterman AL, Stepanov VM, Rudenskaia GN, Khodova OM, Tsaplina IA . [Carboxypeptidase T--intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase] . Biokhimiia . 49 . 2 . 292–301 . February 1984 . 6424730 .
- Smulevitch SV, Osterman AL, Galperina OV, Matz MV, Zagnitko OP, Kadyrov RM, Tsaplina IA, Grishin NV, Chestukhina GG, Stepanov VM . Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity . FEBS Letters . 291 . 1 . 75–8 . October 1991 . 1936254 . 10.1016/0014-5793(91)81107-j .
- Teplyakov A, Polyakov K, Obmolova G, Strokopytov B, Kuranova I, Osterman A, Grishin N, Smulevitch S, Zagnitko O, Galperina O . Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris . European Journal of Biochemistry . 208 . 2 . 281–8 . September 1992 . 1521526 . 10.1111/j.1432-1033.1992.tb17184.x . free .