Information on EC 3.4.17.15 - carboxypeptidase A2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.17.15
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RECOMMENDED NAME
GeneOntology No.
carboxypeptidase A2
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
181186-98-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Hessian fly
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-
Manually annotated by BRENDA team
preprocarboxypeptidase A2; Japanese flounder, female
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
angiotensin II + H2O
angiotensin-(1-7) + L-Phe
show the reaction diagram
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-
-
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?
angiotensin-(1-12) + H2O
angiotensin I + ?
show the reaction diagram
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conversion of Ang-(1-12) to Ang I proceeds through stepwise cleavage of C-terminal Tyr and Leu residues
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?
benzyloxycarbonyl-Gly-Gly-Leu + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Trp + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Tyr + H2O
?
show the reaction diagram
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-
-
-
?
benzyloxycarbonyl-Gly-Phe + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Trp + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Tyr + H2O
?
show the reaction diagram
benzyloxycarbonyl-Val-Phe + H2O
benzyloxycarbonyl-Val + L-Phe
show the reaction diagram
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-
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
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preferred substrate
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
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-
-
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?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
show the reaction diagram
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-
-
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?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
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-
-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme is not involved in development of Silver-Russell syndrome disease
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc-metallopeptidase, binding residues are H69, E72, and H196
additional information
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the enzyme is a metallocarboxypeptidase containing the HXXE motif
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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1 mM, complete inhibition
latexin
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a carboxypeptidase A inhibitor protein, inhibits mast-cell CPA, CPA1, and CPA2, is associated with granular structures distinct from secretory granules and lysosomes in peritoneal mast cells, purification from and expression analysis in peritoneal mast cell granules, overview
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Potato carboxypeptidase inhibitor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.191
angiotensin II
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pH 8.1, 37C
5.3 - 6.53
benzyloxycarbonyl-Gly-Gly-Leu
0.314 - 0.372
benzyloxycarbonyl-Gly-Gly-Phe
0.146
benzyloxycarbonyl-Gly-Gly-Trp
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pH 7.5, 25C
0.125
benzyloxycarbonyl-Gly-Gly-Tyr
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pH 7.5, 25C
2.27
Benzyloxycarbonyl-Gly-Phe
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pH 7.5, 25C
0.127 - 2.028
benzyloxycarbonyl-Gly-Trp
0.145 - 0.175
Benzyloxycarbonyl-Gly-Tyr
0.49
hippuryl-L-phenylalanine
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pH 7.4, 25C, recombinant enzyme
0.016
methotrexate-alpha-(1-naphthyl)alanine
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pH 7.4, 25C, recombinant enzyme
0.056
methotrexate-alpha-phenylalanine
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pH 7.4, 25C, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.8 - 14
benzyloxycarbonyl-Gly-Gly-Leu
58.1 - 90.3
benzyloxycarbonyl-Gly-Gly-Phe
96.9
benzyloxycarbonyl-Gly-Gly-Trp
Rattus norvegicus
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70
benzyloxycarbonyl-Gly-Gly-Tyr
Homo sapiens
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pH 7.5, 25C
16.1 - 16.8
Benzyloxycarbonyl-Gly-Phe
26.6
benzyloxycarbonyl-Gly-Trp
Rattus norvegicus
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9.7 - 14.4
Benzyloxycarbonyl-Gly-Tyr
9.3
hippuryl-L-phenylalanine
Homo sapiens
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pH 7.4, 25C, recombinant enzyme
22
methotrexate-alpha-(1-naphthyl)alanine
Homo sapiens
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pH 7.4, 25C, recombinant enzyme
5.1
methotrexate-alpha-phenylalanine
Homo sapiens
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pH 7.4, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
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purified recombinant enzyme, substrate hippuryl-L-phenylalanine
2800
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purified recombinant enzyme, substrate hippuryl-L-phenyllactate
additional information
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catalytic efficency of the purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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mesenteric arterial bed, enzyme is identical with its pancreatic counterpart
Manually annotated by BRENDA team
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quantitative expression analysis of CPA genes in fetal tissues, overview
Manually annotated by BRENDA team
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80% of toal carboxypeptidas acitivity is located in the gut
Manually annotated by BRENDA team
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peritoneal
Manually annotated by BRENDA team
additional information
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expression analysis in different larval development stages
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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x * 34000, recombinant enzyme, SDS-PAGE
45000
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x * 45000, recombinant proenzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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recombinant enzyme expressed in Pichia pastoris
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method at 4C and at 20C, procarboxypeptidase A2 is crystallized using vapour diffusion approach. The crystals belong to the monoclinic system spacegroup P21 and present one procarboxypeptidase A2 molecule per asymmetric unit
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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half-life of purified recombinant CPA2 is 24 min, and 8fold longer than for CPA1
90
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3 h, denturation, wild-type and mutant enzymes, determination of hydrogen exchange, after 30 min at room temperature prior to 10fold dilution with proton containing buffer, two mutants fail to denature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from mesenteric arterial bed perfusate
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recombinant pro-CPA2 from Saccharomyces cerevisiae by hydrophobic interaction and anion exchange chromatography to homogeneity
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recombinant proenzyme from Pichia pastoris by hydrophobic interaction and anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of the preproenzyme, phylogenetic analysis
DNA and amino acid sequence determination and analysis, expression of the pro-CPA2 in Saccharomyces cerevisiae
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DNA and amino acid sequence determination and analysis, genetic structure, chromosomal localization at 7q32, quantitative expression analysis, low expression level in genomic regions associated with Silver-Russell syndrome disease, overview
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overexpression of the proenzyme in Pichia pastoris
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procarboxypeptidase A2 is expressed in Pichia pastoris
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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differential comparison of the activation domain of the proenzyme with three site-directed mutants of different conformational stability by determination of hydrogen exchange using deuterated MALDI-TOF mass spectrometry, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition
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