Carboxypeptidase T

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Carboxypeptidase T
Identifiers
EC number 3.4.17.18
CAS number 89623-65-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Carboxypeptidase T (EC 3.4.17.18, CPT) is an 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.

References[edit]

  1. ^ Osterman, A.L.; Stepanov, V.M.; Rudenskaya, G.N.; Khodova, O.M.; Tsaplina, I.A.; Yakovleva, M.B.; Loginova, L.G. (1984). "Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases". Biochemistry (Moscow). 49: 292–301. PMID 6424730. 
  2. ^ Smulevitch, S.V.; Osterman, A.L.; Galperina, O.V.; Matz, M.V.; Zagnitko, O.P.; Kadyrov, R.M.; Tsaplina, I.A.; Grishin, N.V.; Chestukhina, G.G.; Stepanov, V.M. (1991). "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity". FEBS Lett. 291: 75–78. doi:10.1016/0014-5793(91)81107-j. PMID 1936254. 
  3. ^ Teplyakov, A.; Polyakov, K.; Obmolova, G.; Strokopytov, B.; Kuranova, I.; Osterman, A.; Grishin, N.; Smulevitch, S.; Zagnitko, O.; Galperina, O.; Matz, M.; Stepanov, V. (1992). "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281–288. doi:10.1111/j.1432-1033.1992.tb17184.x. PMID 1521526. 

External links[edit]