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
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3.4.17.18
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camptothecin
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pressor
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topoisomerase
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children
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pain
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carnitine
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services
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terminology
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percept
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session
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palmitoyltransferase
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surgeon
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postoperative
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sympathetic
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physician
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demographic
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medicare
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reimbursement
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comorbidities
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posttraumatic
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bill
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irinotecan
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topotecan
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veterans
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outpatient
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commission
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insurance
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neuropsychological
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reoperation
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psycinfo
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physiotherapy
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acuminata
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readmission
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payment
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impulsivity
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psychotherapy
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malonyl-coa
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inattention
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handgrip
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cotrimoxazole
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methylphenidate
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cholinephosphotransferase
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event-related
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myoglobinuria
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attention-deficit
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stroop
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icd-9-cm
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degradation
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marketscan
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therapist
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payer
- 3.4.17.18
- camptothecin
-
pressor
-
topoisomerase
- children
- pain
- carnitine
-
services
-
terminology
-
percept
-
session
- palmitoyltransferase
-
surgeon
-
postoperative
-
sympathetic
-
physician
-
demographic
-
medicare
-
reimbursement
-
comorbidities
-
posttraumatic
-
bill
- irinotecan
- topotecan
-
veterans
-
outpatient
-
commission
-
insurance
-
neuropsychological
-
reoperation
-
psycinfo
-
physiotherapy
- acuminata
-
readmission
-
payment
-
impulsivity
-
psychotherapy
- malonyl-coa
-
inattention
-
handgrip
-
cotrimoxazole
- methylphenidate
-
cholinephosphotransferase
-
event-related
- myoglobinuria
-
attention-deficit
-
stroop
-
icd-9-cm
- degradation
-
marketscan
-
therapist
-
payer
Reaction
releases a C-terminal residue, which may be hydrophobic or positively charged =
Synonyms
carboxypeptidase SG, carboxypeptidase T, CPT, metallocarboxypeptidase T
ECTree
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Engineering
Engineering on EC 3.4.17.18 - carboxypeptidase T
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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
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/T257A/D260G/T262D
H68N
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mutant, it is shown that the His68 residue is not a structural determinant of specificity
L254N
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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
G215S/A251G/T257A/D260G/T262D
mutant enzyme in which the amino-acid residues of the S1' subsite are substituted by the corresponding residues from pancreatic carboxypeptidase B. The mutant enzyme retains the broad, mainly hydrophobic selectivity of wild-type enzyme
G215S/A251G/T257A/D260G/T262D
mutant enzyme with the primary specificity pocket fully reproducing the one in pancreatic carboxypeptidase B retains the broad, mainly hydrophobic substrate specificity of the wild-type enzyme