Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.17.1: carboxypeptidase A

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

Word Map on EC 3.4.17.1

Reaction

release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro =

Synonyms

A-type metallocarboxypeptidase, AcCP, Anson's enzyme, ASPA, aspartoacyclase, carboxypeptidase, carboxypeptidase a, carboxypeptidase A-6, carboxypeptidase A-like activity, carboxypeptidase A1, carboxypeptidase A2, Carboxypeptidase A3, carboxypeptidase A4, carboxypeptidase vitellogenic-like, carboxypeptidase-A, carboxypolypeptidase, colon mast cell carboxypeptidase, CPA, CPA1, CPA3, CPA4, CPA6, CPAI, CPD, CPVL, EC 3.4.12.2, EC 3.4.2.1, hCPA, hCPA4, mast cell carboxypeptidase A, mast cell CPA, mast cell-CPA, mast-cell carboxypeptidase A, mast-cell CPA, MC-CP, MC-CPA, MCCPA, MCP-2, mCPA, MDCP-A1, MDCP-A2, MeCPA, MF-CPA, molting carboxypeptidase A, molting fluid carboxypeptidase A, More, Nna1/CCP1, ochratoxin A hydrolytic enzyme, PTD012, RMC-CP, vitellogenic-like carboxypeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.1 carboxypeptidase A

Engineering

Engineering on EC 3.4.17.1 - carboxypeptidase A

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y248A
-
the ratio of turnover number to Km-value with hippuryl-L-Phe as substrate is 113fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with N-[3-(2-furyl)acryloyl]-Phe-Phe as substrate is 262fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate as substrate is 85fold lower than that of the wild-type enzyme. The Ki-value for (2R,3S)-2-benzyl-3,4-epoxybutanoic acid is 3.1fold higher than the wild-type value
Y248F
-
the ratio of turnover number to Km-value with hippuryl-L-Phe as substrate is 49fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with N-[3-(2-furyl)acryloyl]-Phe-Phe as substrate is 49fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate as substrate is 52.4fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with hippuryl-DL-beta-phenyllactate as substrate is 6.5fold lower than that of the wild-type enzyme.The Ki-value for (2R,3S)-2-benzyl-3,4-epoxybutanoic acid is 86% of the wild-type value
A305E
-
tested Canavan Disease mutation, results in undetectable enzyme activity
A57T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
C124A
-
alanine substitution of Cys124, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152A
-
alanine substitution of Cys152, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152W
-
tested Canavan Disease mutation, results in undetectable enzyme activity
C61A
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61S
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61W
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D204H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D249V
-
tested Canavan Disease mutation, results in undetectable enzyme activity
D68A
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E178A
-
mutation of the general proton donor
E214X
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E24D
-
mutation of a putative zinc-binding residue
E24G
-
mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity
E24H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
E24H/H116E
-
mutant designed to switch the order of the zinc-binding residues
E285A
-
tested Canavan Disease mutation
F295S
-
untested Canavan Disease mutation, results in undetectable enzyme activity
G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
H116E
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
H116G
-
mutation of a putative zinc-binding residue
H21E/E24H
-
mutant designed to switch the order of the zinc-binding residues
H21G
-
mutation of a putative zinc-binding residue
H21P
-
untested Canavan Disease mutation, results in undetectable enzyme activity
I143T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
K213E/G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
M195R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
P183H
-
untested Canavan Disease mutation
R127A
-
the mutation causes kcat to decrease from 12 to 0.012 which corresponds to a 6 kcal/mol decrease in the stabilization of transition state in the rate determining step
R63N
-
mutation that affects transition state stabilization
R71N
-
mutation that affects substrate carboxyl binding
E378A
-
Glu378 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L
-
Tyr356 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L/E378A
-
mutant expresses about 80% of the amount of Mc-cpa compared to the wild type enzyme, the mutant enzyme lacks activity
additional information