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Information on EC 3.4.17.15 - carboxypeptidase A2 and Organism(s) Homo sapiens and UniProt Accession P48052
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3.4.17.15 carboxypeptidase A2Specify your search results
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPA2
CPA2
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
181186-98-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
preferred substrate
-
-
?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is not involved in development of Silver-Russell syndrome disease
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is not involved in development of Silver-Russell syndrome disease
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
potato carboxypeptidase inhibitor
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
structure of the activation domain of the procarboxypeptidase A2, activation mechanism, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
quantitative expression analysis of CPA genes in fetal tissues, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CBPA2_HUMAN
419
0
47030
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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
-
structure-function relationship, three-dimensional structure, secondary structure, NMR analysis at pH 7.0, 25°C, hydrogen exchange analysis in unfolding, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
proteolytic modification
-
the proCPA2 is activated by cleavage by trypsin
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
half-life of purified recombinant CPA2 is 24 min, and 8fold longer than for CPA1
90
-
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
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, 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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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