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3.4.17.18: carboxypeptidase T

This is an abbreviated version!
For detailed information about carboxypeptidase T, go to the full flat file.

Word Map on EC 3.4.17.18

Reaction

releases a C-terminal residue, which may be hydrophobic or positively charged =

Synonyms

carboxypeptidase SG, carboxypeptidase T, CPT, metallocarboxypeptidase T

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.18 carboxypeptidase T

Engineering

Engineering on EC 3.4.17.18 - carboxypeptidase T

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A243G
successive substitution of residues in the CpT S1'-subsite by similar residues of CpB, retains substrate specificity of the wild-type
A243G/D253G/T255D
successive substitution of residues in the CpT S1'-subsite by similar residues of CpB, retains substrate specificity of the wild-type
D253G/T255D
successive substitution of residues in the CpT S1'-subsite by similar residues of CpB, retains substrate specificity of the wild-type
D260G
mutant, the influence of residues at positions 260 and 262 on a broad substrate specificity is studied
D260G/T262I
mutant, the influence of residues at positions 260 and 262 on a broad substrate specificity is studied
D260G/T262K
mutant, the influence of residues at positions 260 and 262 on a broad substrate specificity is studied
D260G/T262R
mutant, the influence of residues at positions 260 and 262 on a broad substrate specificity is studied
D260N
decrease in activity with both substrates benzyloxycarbonyl-Ala-Ala-Leu and benzyloxycarbonyl-Ala-Ala-Arg
D263N
mutant acquires carboxypeptidase A-like selectivity
G207S/A243G/D253G/T255D
successive substitution of residues in the CpT S1'-subsite by similar residues of CpB, retains substrate specificity of the wild-type
G207S/A243G/T250A/D253G/T255D
successive substitution of residues in the CpT S1'-subsite by similar residues of CpB, retains substrate specificity of the wild-type
G215S/A251G/D253_L254insT/T257A/D260G/T262D
mutant CPT6
G215S/A251G/T257A/D260G/T262D
H68N
-
mutant, it is shown that the His68 residue is not a structural determinant of specificity
L211Q
mutant acquires carboxypeptidase B-like properties
L254N
-
mutant, hydrolysis efficiency of substrates with C-terminal Leu and Arg not changed, 28-fold decrease in activity towards the substrate with C-terminal Glu
L254S
increase in activity with both substrates benzyloxycarbonyl-Ala-Ala-Leu and benzyloxycarbonyl-Ala-Ala-Arg
T257D
decrease in activity with substrate benzyloxycarbonyl-Ala-Ala-Leu, increase in activity with substrate benzyloxycarbonyl-Ala-Ala-Arg
T262G
increase in catalytic activity