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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
Synonyms
carboxypeptidase a2,
more
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CPA2
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Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
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Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
residues Glu270 and Arg127 are important for activity, the catalytic triad consists of Ile275, Tyr248, and Ala250, residues at positions 202, 254, and 268 are important for substrate specificity
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
structure-function relationship, activation mechanism
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hydrolysis of peptide bond
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angiotensin II + H2O
angiotensin-(1-7) + L-Phe
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?
angiotensin-(1-12) + H2O
angiotensin I + ?
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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
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
benzyloxycarbonyl-Gly-Gly-Trp + H2O
?
benzyloxycarbonyl-Gly-Gly-Tyr + H2O
?
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-
-
-
?
benzyloxycarbonyl-Gly-Phe + H2O
?
benzyloxycarbonyl-Gly-Trp + H2O
?
benzyloxycarbonyl-Gly-Tyr + H2O
?
benzyloxycarbonyl-Val-Phe + H2O
benzyloxycarbonyl-Val + L-Phe
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-
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?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
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preferred substrate
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?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
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?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
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-
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?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
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-
?
additional information
?
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benzyloxycarbonyl-Gly-Gly-Leu + H2O
?
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?
benzyloxycarbonyl-Gly-Gly-Leu + H2O
?
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?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
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?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
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?
benzyloxycarbonyl-Gly-Gly-Trp + H2O
?
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?
benzyloxycarbonyl-Gly-Gly-Trp + H2O
?
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?
benzyloxycarbonyl-Gly-Phe + H2O
?
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?
benzyloxycarbonyl-Gly-Phe + H2O
?
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?
benzyloxycarbonyl-Gly-Trp + H2O
?
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?
benzyloxycarbonyl-Gly-Trp + H2O
?
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?
benzyloxycarbonyl-Gly-Tyr + H2O
?
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?
benzyloxycarbonyl-Gly-Tyr + H2O
?
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?
additional information
?
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no measurable activity with benzyloxycarbonyl-Gly-Gly-Val, benzyloxycarbonyl-Gly-Gly-Ala und benzyloxycarbonyl-Gly-Gly-Ser. CPA2 is the only reported carboxypeptidase with specificity for C-terminal Trp residues
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?
additional information
?
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the enzyme is not involved in development of Silver-Russell syndrome disease
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?
additional information
?
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carboxy-terminal amino acids with aromatic or branched aliphatic side chains are preferred
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?
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additional information
?
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the enzyme is not involved in development of Silver-Russell syndrome disease
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?
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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
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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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potato carboxypeptidase inhibitor
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determination of hydrogen exchange in the slow exchange core of the inhibitor in different conformational stages using deuterated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, overview
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potato carboxypeptidase inhibitor
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10 microM, complete inhibition
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additional information
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structure of the activation domain of the procarboxypeptidase A2, activation mechanism, overview
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additional information
the triad for binding of the activation peptide consists of Asp, Phe, and Trp residues
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Pancreatitis
Clinical and Genetic Risk Factors for Acute Pancreatitis in Patients With Acute Lymphoblastic Leukemia.
Pancreatitis
The proteome of mesenteric lymph during acute pancreatitis and implications for treatment.
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0.191
angiotensin II
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pH 8.1, 37°C
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, 25°C
0.125
benzyloxycarbonyl-Gly-Gly-Tyr
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pH 7.5, 25°C
2.27
Benzyloxycarbonyl-Gly-Phe
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pH 7.5, 25°C
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, 25°C, recombinant enzyme
0.016
methotrexate-alpha-(1-naphthyl)alanine
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pH 7.4, 25°C, recombinant enzyme
0.056
methotrexate-alpha-phenylalanine
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pH 7.4, 25°C, recombinant enzyme
5.3
benzyloxycarbonyl-Gly-Gly-Leu
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pH 7.5, 25°C
6.53
benzyloxycarbonyl-Gly-Gly-Leu
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0.314
benzyloxycarbonyl-Gly-Gly-Phe
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0.372
benzyloxycarbonyl-Gly-Gly-Phe
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pH 7.5, 25°C
0.127
benzyloxycarbonyl-Gly-Trp
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0.261
benzyloxycarbonyl-Gly-Trp
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pH 7.5, 25°C
2.028
benzyloxycarbonyl-Gly-Trp
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pH 7.5, 25°C
0.145
Benzyloxycarbonyl-Gly-Tyr
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0.175
Benzyloxycarbonyl-Gly-Tyr
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pH 7.5, 25°C
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11.8 - 14
benzyloxycarbonyl-Gly-Gly-Leu
58.1 - 90.3
benzyloxycarbonyl-Gly-Gly-Phe
96.9
benzyloxycarbonyl-Gly-Gly-Trp
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70
benzyloxycarbonyl-Gly-Gly-Tyr
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pH 7.5, 25°C
16.1 - 16.8
Benzyloxycarbonyl-Gly-Phe
26.6
benzyloxycarbonyl-Gly-Trp
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9.7 - 14.4
Benzyloxycarbonyl-Gly-Tyr
9.3
hippuryl-L-phenylalanine
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pH 7.4, 25°C, recombinant enzyme
22
methotrexate-alpha-(1-naphthyl)alanine
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pH 7.4, 25°C, recombinant enzyme
5.1
methotrexate-alpha-phenylalanine
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pH 7.4, 25°C, recombinant enzyme
11.8
benzyloxycarbonyl-Gly-Gly-Leu
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pH 7.5, 25°C
14
benzyloxycarbonyl-Gly-Gly-Leu
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58.1
benzyloxycarbonyl-Gly-Gly-Phe
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pH 7.5, 25°C
90.3
benzyloxycarbonyl-Gly-Gly-Phe
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pH 7.5, 25°C
16.1
Benzyloxycarbonyl-Gly-Phe
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pH 7.5, 25°C
16.8
Benzyloxycarbonyl-Gly-Phe
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9.7
Benzyloxycarbonyl-Gly-Tyr
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pH 7.5, 25°C
14.4
Benzyloxycarbonyl-Gly-Tyr
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2800
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purified recombinant enzyme, substrate hippuryl-L-phenyllactate
8.7
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purified recombinant enzyme, substrate hippuryl-L-phenylalanine
additional information
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catalytic efficency of the purified recombinant enzyme
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Hessian fly
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brenda
preprocarboxypeptidase A2; Japanese flounder, female
SwissProt
brenda
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brenda
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UniProt
brenda
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brenda
male wistar rat
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brenda
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mesenteric arterial bed, enzyme is identical with its pancreatic counterpart
brenda
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brenda
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quantitative expression analysis of CPA genes in fetal tissues, overview
brenda
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brenda
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brenda
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80% of toal carboxypeptidas acitivity is located in the gut
brenda
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peritoneal
brenda
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brenda
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brenda
additional information
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expression analysis in different larval development stages
brenda
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brenda
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brenda
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brenda
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CBPA2_HUMAN
419
0
47030
Swiss-Prot
Secretory Pathway (Reliability: 1 )
CBPA2_MOUSE
417
0
47057
Swiss-Prot
Secretory Pathway (Reliability: 2 )
CBPA2_RAT
417
0
46912
Swiss-Prot
Secretory Pathway (Reliability: 1 )
A0A072V396_MEDTR
434
0
49244
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A7R8CET7_LEPSM
430
0
48693
TrEMBL
other Location (Reliability: 5 )
A0A812EW62_SEPPH
453
0
52794
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A8B6DMC1_MYTGA
649
0
73457
TrEMBL
other Location (Reliability: 2 )
A0A6J8CK49_MYTCO
346
0
39678
TrEMBL
other Location (Reliability: 1 )
A0A8M1N162_DANRE
422
0
47935
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A6J8EHA7_MYTCO
437
0
49226
TrEMBL
Secretory Pathway (Reliability: 2 )
Q6GMH9_DANRE
417
0
46974
TrEMBL
Secretory Pathway (Reliability: 1 )
Q8AXN5_PAROL
419
0
47743
TrEMBL
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34000
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x * 34000, recombinant enzyme, SDS-PAGE
45000
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x * 45000, recombinant proenzyme, SDS-PAGE
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?
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x * 34000, recombinant enzyme, SDS-PAGE
?
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x * 45000, recombinant proenzyme, SDS-PAGE
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
additional information
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structure-function relationship, three-dimensional structure, secondary structure, NMR analysis at pH 7.0, 25°C, hydrogen exchange analysis in unfolding, overview
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glycoprotein
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recombinant enzyme expressed in Pichia pastoris
proteolytic modification
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synthesized as procarboxypeptidase A2
proteolytic modification
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the proCPA2 is activated by cleavage by trypsin
proteolytic modification
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the proCPA2 is activated by proteoltyic cleavage
proteolytic modification
in silico conversion of zymogen into the primary cleavage state using available X-ray structures to investigate its spontaneous dissociation process of the prosegment from its associated enzyme domain using steered molecular dynamics simulation. The cleavage substantially destabilizes most of the hydrogen bonds at the prosegment-enzyme interface. During prosegment unbinding, the enzyme shows first rupture in the globular domain and then in the connecting segment
proteolytic modification
the proCPA2 is activated by proteoltyic cleavage
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hanging drop vapour diffusion method at 4°C and at 20°C, 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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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
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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
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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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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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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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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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Gardell, S.J.; Craik, C.S.; Clauser, E.; Goldsmith, E.J.; Stewart, C.B.; Graf, M.; Rutter, W.J.
A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family
J. Biol. Chem.
263
17828-17836
1988
Rattus norvegicus
brenda
Reverter, D.; Garcia-Saez, I.; Catasus, L.; Vendrell, J.; Coll, M.; Aviles, F.X.
Characterization and preliminary x-ray diffraction analysis of human pancreatic procarboxypeptidase A2
FEBS Lett.
420
7-10
1997
Homo sapiens
brenda
Laethem, R.M.; Blumenkopf, T.A.; Cory, M.; Elwell, L.; Moxham, C.P.; Ray, P.H.; Walton, L.M.; Smith, G.K.
Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2
Arch. Biochem. Biophys.
332
8-18
1996
Homo sapiens
brenda
Uratani, Y.; Takiguchi-Hayashi, K.; Miyasaka, N.; Sato, M.; Jin, M.; Arimatsu, Y.
Latexin, a carboxypeptidase A inhibitor, is expressed in rat peritoneal mast cells and is associated with granular structures distinct from secretory granules and lysosomes
Biochem. J.
346
817-826
2000
Rattus norvegicus
brenda
Srivastava, A.S.; Kurokawa, T.; Suzuki, T.
Molecular cloning and cDNA sequence analysis of carboxypeptidases A1, A2 and B from the Japanese flounder Paralichthys olivaceus
Comp. Biochem. Physiol. B
135
593-599
2003
Paralichthys olivaceus (Q8AXN5)
brenda
Villanueva, J.; Canals, F.; Villegas, V.; Querol, E.; Aviles, F.X.
Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins
FEBS Lett.
472
27-33
2000
Homo sapiens
brenda
Liu, X.; Fellers, J.P.; Zhu, Y.C.; Mutti, N.S.; El-Bouhssini, M.; Chen, M.S.
Cloning and characterization of cDNAS encoding carboxypeptidase-like proteins from the gut of Hessian fly larvae Mayetiola destructor (Say)
Insect Biochem. Mol. Biol.
36
665-673
2006
Mayetiola destructor
brenda
Reverter, D.; Ventura, S.; Villegas, V.; Vendrell, J.; Aviles, F.X.
Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway
J. Biol. Chem.
273
3535-3541
1998
Homo sapiens
brenda
Bentley, L.; Nakabayashi, K.; Monk, D.; Beechey, C.; Peters, J.; Birjandi, Z.; Khayat, F.E.; Patel, M.; Preece, M.A.; Stanier, P.; Scherer, S.W.; Moore, G.E.
The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate for Silver-Russell syndrome
J. Med. Genet.
40
249-256
2003
Homo sapiens
brenda
Jimenez, M.A.; Villegas, V.; Santoro, J.; Serrano, L.; Vendrell, J.; Aviles, F.X.; Rico, M.
NMR solution structure of the activation domain of human procarboxypeptidase A2
Protein Sci.
12
296-305
2003
Homo sapiens
brenda
Jitonnom, J.; Sontag, C.
Comparative study on activation mechanism of carboxypeptidase A1, A2 and B: first insights from steered molecular dynamics simulations
J. Mol. Graph. Model.
38
298-303
2012
Homo sapiens (P48052)
brenda
Pereira, H.; Souza, L.; Costa-Neto, C.; Salgado, M.; Oliveira, E.
Carboxypeptidases A1 and A2 from the perfusate of rat mesenteric arterial bed differentially process angiotensin peptides
Peptides
33
67-76
2012
Rattus norvegicus
brenda
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