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3.4.16.5: carboxypeptidase C

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

Word Map on EC 3.4.16.5

Reaction

release of a C-terminal amino acid with broad specificity =

Synonyms

A-type metallocarboxypeptidase, acidic serine carboxypeptidase, AtCPY, BRS1, carboxypeptidase a, carboxypeptidase A4, carboxypeptidase C, Carboxypeptidase II, carboxypeptidase Y, carboxypeptidase YSCY, carboxypeptidase-Y, Case, CatA, CathA, cathepsin A, CaY, CP-MI, CP-MIII, CP-WIII, CPA4, CPase, CPC, CPD-Y, CPW, CPY, Cpy1p, CTSA, Cxp1, deamidase, EC 3.4.12.1, EC 3.4.16.1, EC 3.4.16.3, hCath A, HPP, lysosomal carboxypeptidase A, lysosomal protective protein, MO54, More, MpiCP-1, MpiCP-2, Phaseolin, PpcA, PRC1, proCPY, protective protein cathepsin A, protective protein/cathepsin A, retinoid-inducible serine carboxypeptidase, SCP, Scpep1, Ser carboxypeptidase, Ser carboxypeptidase-like protein, serine carboxypeptidase, serine carboxypeptidase 1, serine carboxypeptidase I, serine carboxypeptidase Scpep1, SmSCP-1, TcCBP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.5 carboxypeptidase C

Engineering

Engineering on EC 3.4.16.5 - carboxypeptidase C

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A251E
the mutant shows increased activity compared to the wild type cathepsin A
K355Q
the mutant shows increased activity compared to the wild type cathepsin A
L354D
the mutant shows decreased activity compared to the wild type cathepsin A
P451A
the mutant shows increased activity compared to the wild type cathepsin A
R20A
the mutant shows decreased activity compared to the wild type cathepsin A
R262A/R292A
double mutant also undergoes processing to form large and small subunits, suggesting alternative avenues for the maturation of cathepsin A
R344A
the mutant shows about wild type cathepsin A activity
R344D
inactive mutant, the 54 kDa precursor/zymogen with the R344D substitution is not processed to the 32/20 kDa mature form with CathA activity
R344E
the mutant shows reduced cathepsin A activity compared to the wild type
R344G
the mutant shows reduced cathepsin A activity compared to the wild type
R344I
the mutant shows reduced cathepsin A activity compared to the wild type
R344K
the mutant shows reduced cathepsin A activity compared to the wild type
R344M
the mutant shows reduced cathepsin A activity compared to the wild type
R344N
the mutant shows reduced cathepsin A activity compared to the wild type
R344P
the mutant shows reduced cathepsin A activity compared to the wild type
R344Q
the mutant shows reduced cathepsin A activity compared to the wild type
R344S
the mutant shows about wild type cathepsin A activity
R344V
the mutant shows reduced cathepsin A activity compared to the wild type
S150A/R284A/R298A
triple mutant S150A/R284A/R298A also undergoes cleavage into large and small subunits, comparable with the wildtype cathepsin A, suggesting that these sites are not mandatory for the activation of cathepsin A
W382A
the mutant shows decreased activity compared to the wild type cathepsin A
T343F
-
the mutant accumulates in the microsomal fraction of protoplasts treated with 2-mercaptoethanol and is for the most part susceptible to digestion by endoglycosidase H
C341F
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341G
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu and benzyloxycarbonyl-Gly-Phe, somewhat increased ratio with benzyloxycarbonyl-Ala-Phe
C341S
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341V
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
E355A
-
no CPY secretion
E355Q
-
mutant shows moderate CPY secretion
E365A
-
mutant shows moderate CPY secretion
E369A
-
mutant shows moderate CPY secretion
E371A
-
mutant shows CPY secretion similar to the wild type
F367L
-
no CPY secretion
G255R
-
PNGase releases N-glycans from the mutant during the endoplasmic reticulum-associated degradation process in vivo. A major endoproteolytic reaction on the mutant appears to occur between amino acid 400 and 404
L267A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 18.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 113% for furylacryloyl-Ala-Lys, 130% for furylacryloyl-Ala-Arg,10.8% for furylacryloyl-Phe-Ala, 18.5% for furylacryloyl-Phe-Val and 31.3% for furylacryloyl-Phe-Leu
L267D
-
mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1'
L267D/L272A
L267D/L272D
-
mutant enzyme with a preference for substrates with C-terminal basic amino acid residues
L267E
-
mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1'
L267F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 88.5% for furylacryloyl-Ala-Leu, 65.2% for furylacryloyl-Ala-Glu, 44% for furylacryloyl-Ala-Lys, 53% for furylacryloyl-Ala-Arg, 34.2% for furylacryloyl-Phe-Ala, 57.8% for furylacryloyl-Phe-Val and 82.6% for furylacryloyl-Phe-Leu
L267K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L267Q
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 17% for furylacryloyl-Ala-Leu, 48% for furylacryloyl-Ala-Glu, 157% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg
L267R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L272A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 8.7% for furylacryloyl-Ala-Leu, 60.9% for furylacryloyl-Ala-Glu, 127% for furylacryloyl-Ala-Lys, 47% for furylacryloyl-Ala-Arg, 78.9% for furylacryloyl-Phe-Ala, 50% for furylacryloyl-Phe-Val and 15.6% for furylacryloyl-Phe-Leu
L272D
L272E
L272F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 83% for furylacryloyl-Ala-Leu, 95.7% for furylacryloyl-Ala-Glu, 46% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg, 113% for furylacryloyl-Phe-Ala, 121% for furylacryloyl-Phe-Val and 83.4% for furylacryloyl-Phe-Leu
L272K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L272Q
L272R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L272R/M398F
L272R/T60F
N356A
-
mutant shows CPY secretion similar to the wild type
N87I
-
mutant enzyme with reduced transport rate and reduced enzymatic activity, 30%
S297A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 39.7% for furylacryloyl-Ala-Leu, 161% for furylacryloyl-Ala-Glu, 66% for furylacryloyl-Ala-Lys, 80% for furylacryloyl-Ala-Arg, 126% for furylacryloyl-Phe-Ala, 109% for furylacryloyl-Phe-Val and 88.6% for furylacryloyl-Phe-Leu
S297D
S297E
S297F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 43.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 42% for furylacryloyl-Ala-Lys, 6.7% for furylacryloyl-Ala-Arg, 86.8% for furylacryloyl-Phe-Ala, 55% for furylacryloyl-Phe-Val and 60.9% for furylacryloyl-Phe-Leu
S297K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
S297Q
S297R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
T60F/L267D/L272A
Y361F
-
no CPY secretion
nutrition
-
the enzyme can be used to eliminate the bitterness of bitter peptides
additional information