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Carboxypeptidase T

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Carboxypeptidase T
Identifiers
EC no.3.4.17.18
CAS no.89623-65-4
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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

  1. ^ Osterman, A.L., Stepanov, V.M., Rudenskaya, G.N., Khodova, O.M., Tsaplina, I.A., Yakovleva, M.B. and 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  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. and 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Teplyakov, A., Polyakov, K., Obmolova, G., Strokopytov, B., Kuranova, I., Osterman, A., Grishin, N., Smulevitch, S., Zagnitko, O., Galperina, O., Matz, M. and 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)