Literature summary for 3.4.17.18 extracted from

Timofeev, V.I.; Kuznetsov, S.A.; Akparov, V.K.h.; Chestukhina, G.G.; Kuranova, I.P.
Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine (2013), Biochemistry (Moscow), 78, 252-259.

Search for more literature for 3.4.17.18

Cloned(Commentary)

Cloned (Comment)	Organism
-	Thermoactinomyces vulgaris

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with N-benzyloxycarbonyl-L-leucine, at 1.38 A resolution. The structure of the complex is almost identical to that of the free carboxypeptidase T molecule, and a SO42- ion is also localized in the active site. The S1 subsite of carboxypeptidase T is a very conservative structure and negligibly differs from corresponding sites of carboxypeptidase A and carboxypeptidase B in the composition and the 3D structure. The S1 subsite is close to the catalytic zinc ion and to the residues Arg71, Arg147, Arg129, and Glu277 important for catalysis	Thermoactinomyces vulgaris

Crystallization (Comment)

Organism

in complex with N-benzyloxycarbonyl-L-leucine, at 1.38 A resolution. The structure of the complex is almost identical to that of the free carboxypeptidase T molecule, and a SO42- ion is also localized in the active site. The S1 subsite of carboxypeptidase T is a very conservative structure and negligibly differs from corresponding sites of carboxypeptidase A and carboxypeptidase B in the composition and the 3D structure. The S1 subsite is close to the catalytic zinc ion and to the residues Arg71, Arg147, Arg129, and Glu277 important for catalysis

Thermoactinomyces vulgaris

Organism

Organism	UniProt	Comment	Textmining
Thermoactinomyces vulgaris	P29068	-	-

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Release 2023.1 (January 2023)