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Information on EC 3.4.17.1 - carboxypeptidase A and Organism(s) Bos taurus and UniProt Accession P00730
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3.4.17.1 carboxypeptidase ASpecify your search results
Word Map
- 3.4.17.1
- agonist
-
cerebellopontine
- cyclophosphamide
-
cyclopiazonic
- nerve
- artery
-
cyproterone
- pulmonary
-
n6-cyclopentyladenosine
-
cryoprotective
-
cryopreservation
-
resect
-
postoperative
-
hearing
-
facial
-
sarcoplasmic
-
cranial
- aspergillosis
-
vestibular
- schwannomas
-
aversion
-
auditory
- meningioma
- ca2+-atpase
- dpcpx
-
cardiopulmonary
-
preoperative
-
acoustic
-
antiandrogenic
-
vitrification
-
fossa
-
resuscitation
- rantes
-
ryanodine
-
ca2+-free
-
craniotomy
-
epidermoids
- chymase
- serca
- hirsutism
- neuralgia
-
post-thawing
- lipoma
- 2-chloroadenosine
- tinnitus
-
radiosurgery
- vertigo
-
mip-1beta
-
hemifacial
- pharmacology
- drug development
-
out-of-hospital
- biotechnology
- medicine
- analysis
- synthesis
- food industry
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cpa, carboxypeptidase a, mcp-2, mc-cpa, carboxypeptidase a1, carboxypeptidase a3, carboxypeptidase-a, mast cell carboxypeptidase a, carboxypeptidase a4, mecpa, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase a
-
-
Carboxypeptidase A3
-
-
-
-
carboxypolypeptidase
-
-
-
-
CPA
-
-
MC-CPA
-
-
-
-
RMC-CP
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
mechanism
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
relationships between structure and mechanism, zinc environment and substrate complexes
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
mechanisms elucidated from complex with inactivator 2-benzyl-3-iodo-propanoic acid
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
pK values of active site residues, analysis of kinetics and mechanism under alkaline conditions
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
molecular dynamics characterization of active cavity
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
conceptual model of relationship between activity, mechanism and conformational mobility
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CySO3H, S-carboxymethylcysteine, not released: Pro, Hyp, Arg
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
evidence of general base pathway
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
relationships between structure and mechanism, different catalytic sites for esters and peptides, role of mechanic strain discussed
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
correlations between mechanism, kinetics, and structure, intermediates and rate-determining steps
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
evidence for acyl-enzyme intermediates
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
cryospectrokinetic characterization of intermediates, time-course of reaction
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
promoted water pathway, mechanistic model
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
catalytic mechanism involving the Zn2+ ion and residue Glu270 with ester or protein substrates, the tetrahydrate transition state is stabilized by Arg127, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
11075-17-5
-
9031-98-5
-
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-L-Phe + H2O
hippuric acid + L-phenylalanine
the hydrolysis of the hippuryl-L-Phe molecule by carboxypeptidase A is investigated using both density functional theory and a hybrid quantum mechanical/molecular mechanical approach. The enzymatic reaction is found to proceed via a promoted water pathway with Glu270 serving as the general base and general acid. Free-energy calculations indicate that the first nucleophilic addition step is rate-limiting, with a barrier of 17.9 kcal/mol. Besides activating the zinc-bound water nucleophile, the zinc cofactor also serves as an electrophilic catalyst that stabilizes the substrate carbonyl oxygen during the formation of the tetrahedral intermediate. In the Michaelis complex, Arg127, rather than Zn(II), is responsible for the polarization of the substrate carbonyl and it also serves as the oxyanion hole
-
-
?
O-(trans-4-chlorocinnamoyl)-L-beta-phenyllactate + H2O
trans-4-chlorocinnamic acid + L-phenyllactic acid
-
-
-
?
4-chlorocinnamoyl-L-beta-phenyllactate + H2O
4-chlorocinnamic acid + L-beta-phenyllactate
-
-
-
-
?
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-L-beta-phenyllactate + H2O
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala + L-beta-phenyllactate
-
-
-
ir
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe + H2O
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala + L-Phe
-
-
-
ir
carbobenzyloxy-Gly-hippuryl-L-Phe + H2O
carbobenzyloxy-Gly-hippuric acid + L-Phe
-
-
-
ir
glycyl-L-serylglycyl-L-seryl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-seryl-L-tryptophan + H2O
glycyl-L-serylglycyl-L-seryl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-serine + L-tryptophan
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
assay substrate
-
-
?
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-((2-naphthoyl)amino) cinnamate
-
-
-
ir
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-(acetylamino)cinnamate
-
-
-
ir
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-(benzoylamino)-cinnamate
-
-
-
ir
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-tryptophan + H2O
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycine + L-tryptophan
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycylglycyl-L-tryptophan + H2O
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycylglycine + L-tryptophan
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
N-(trans-3-indoleacryloyl)-L-Phe + H2O
trans-3-indoleacrylate + L-Phe
-
-
-
ir
N-[3-(2-furyl)acryloyl]-Phe-Phe + H2O
N-[3-(2-furyl)acryloyl]-Phe + Phe
-
-
-
?
N-[3-(2-furyl)]acryloyl-L-Phe-L-Phe + H2O
N-[3-(2-furyl)]acryloyl-L-Phe + L-Phe
-
-
-
?
N2acetyl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginyl-L-tryptophan + H2O
N2-acetyl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparagine + L-tryptophan
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
peptidyl-L-amino acid + H2O
?
-
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CysSO3, S-carboxymethylcysteine, not released: Pro, hydroxyproline, Arg, enzyme generally releases C-terminal amino acids, with the exception of C-terminal arginine, lysine and proline
-
-
?
additional information
?
-
-
human haemoglobin, removal of specific C-terminal residues
-
-
?
additional information
?
-
-
chicken gizzard tropomyosin, effects on interaction between tropomyosin and actomyosin ATPase
-
-
?
additional information
?
-
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
?
additional information
?
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
?
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
peptidyl-L-amino acid + H2O
?
-
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CysSO3, S-carboxymethylcysteine, not released: Pro, hydroxyproline, Arg, enzyme generally releases C-terminal amino acids, with the exception of C-terminal arginine, lysine and proline
-
-
?
additional information
?
-
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
?
additional information
?
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Mn2+
Ni2+
Zn2+
Co2+
-
X-ray absorption fine study of Co environment in active site, comparison to Zn metalloenzyme
Zn2+
-
Zn enhances kinetic inhibition by imidazole 560fold due to formation of ternary complexes with enzyme
Zn2+
-
X-ray absorption fine study of Zn environment in active site, comparison to Co metalloenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Cys
binds tightly to the active site zinc. D-Cys binds the active site zinc with a sulfur ligand and forms additional interactions with surrounding side chains of the enzyme. D-Cys binding induces a concerted motion of the side chains around the sinc ion
latexin
from mouse recombinantly expressed as His-tagged enzyme in Escherichia coli and purified, overview, analysis of complex formation with CPAI, overview
-
tick carboxypeptidase inhibitor
i.e. TCI, a 75 amino acid, two-domain protein from the blood-sucking tick Rhipcephalus bursa, recombinantly expressed in Escherichia coli and purified, three-dimensional structure of the enzyme-inhibitor protein complex, inhibitor binding and inhibition mechanism, overview
-
(2S)-2-([hydroxy[(1R)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPro2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. I-beta-Ala2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IAla2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPhe2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IGly2
(2S)-2-([hydroxy[(1S)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPro1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. I-beta-Ala1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IAla1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPhe1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IGly1
(2S)-2-[(hydroxy[(1R)-1-[(1,4,7,10-tetraazacyclododecan-1-ylacetyl)amino]ethyl]phosphoryl)oxy]-3-phenylpropanoic acid
-
i.e. I2
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
2-benzyl-3-iodo-propanoic acid
-
mechanisms elucidated from complex with inactivator
alpha-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid
-
all four stereoisomers inhibit in a time dependent manner, inhibited enzyme does not regain its enzymatic activity upon dialysis, inactivation is prevented by 2-benzylsuccinic acid
imidazole
-
Zn2+ enhances kinetic inhibition by imidazole 560fold due to formation of ternary complexes with enzyme
leech carboxypeptidase inhibitor
-
LCI, tight-binding, competitive inhibition, the inhibitor contains four disulfide bonds, biding structure with CPA, oxidative folding pathway and intermediate of wild-type and mutant C19A/C43A mutant, determination of thermodynamics and conformational stability of wild-type and mutant enzymes at pH 8.4/high concentration of DTT, overview
-
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1R)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
i.e. IGlyGly2
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1S)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
i.e. IGlyGly1
N-(2-chloroethyl)-N-methylphenylalanine
-
both enantiomers, computational analysis of the mechanism for reactive inhibition, quantum mechanical and molecular mechanical methods, the inhibitor enantiomers both bind at the active site and perform nucleophilic deactivation involving cofactor Zn2+, overview
O-(hydroxyacetyl)-beta-phenyllactate
-
irreversible inactivation, Kinact/Ki: 57 M-1s-1
O-[[(1R)-(N-phenylmethoxycarbonyl)-L-alanyl]aminoethyl]hydroxyphosphinyl-L-3-phenyllactate
-
(R)-2-benzyl-3-nitropropanoic acid
-
X-ray crystallography discloses that the nitro group well mimics the transition state occurred in the hydrolysis catalyzed by CPA, that is, an O,O'-bidentate coordination to the zinc ion and the two respective hydrogen bonds with Glu-270 and Arg-127. Because the nitro group is a planar species, (R)-2-benzyl-3-nitropropanoic acid is as a pseudo-transition-state analog inhibitor against CPA
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
i.e. IIle1
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
i.e. IIle2
Carbobenzoxyglycine
-
activator of dipeptide hydrolysis, inhibitor of tripeptide hydrolysis, Ki: 27 mM
D-penicillamine
-
catalyzes Zn2+ transfer from carboxypeptidase A to chelators, catalytic chelation
potato carboxypeptidase inhibitor
-
molecular weight 38000, detailed study of inhibitor effects, stability, physical properties, purification protocol
-
potato carboxypeptidase inhibitor
-
i.e. PCI, wild-type and several mutants, oxidative folding, hydrogen exchange, and conformational stability, overview, secondary contact binding site structure and mechanism dependent, recombinant expression of the inhibitor protein in Escherichia coli, overview, steady-state binding kinetics
-
additional information
-
substrate inhibition by: carbobenzoxy-Glyl-L-Phe, benzoyl-Gly-Phe
-
additional information
-
molecular dynamics characterization of inhibitor adducts and structural variations induced by inhibitors
-
additional information
-
analysis of interactions between enzyme and multiple inhibitors using combination plots
-
additional information
-
study about coordination of low molecular weight inhibitors to metal ion
-
additional information
-
no inhibition by (2R,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
additional information
-
no inhibition by erythro-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
additional information
-
no inhibition by N-(aminocarbonyl)phenylalanine up to 3.6 mM
-
additional information
-
rational design of mechanism-based irreversible enzyme inhibitors, inhibition mechanism, overview
-
additional information
-
synthesis of cyclen-containing inhibitors specific for CPA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the capacity of poloxamer 188 to suppress aggregation of denaturated carboxypeptidase A is compared to that of polyethylenglycol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248A
5.8
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248F
120
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, wild-type enzyme
additional information
additional information
-
comparison of Km-values in crystals and in solution
-
additional information
additional information
-
comparison of affinities of various substituted metalloenzymes
-
additional information
additional information
-
comparison of Km-values of enzyme crystals and solution
-
additional information
additional information
-
derivation from classical Michalis-Menten kinetics with some substrates
-
additional information
additional information
-
dissociation constant of enzyme GlyTyr complex: 0.001, no Michaelis-Menten kinetics with some substrates, larger substrates tend to have smaller Km-values than smaller substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
comparison of turnover numbers of enzyme crystals and solution
-
0.11
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, wild-type enzyme
0.27
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248F
0.56
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248A
6.08
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248A
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00043
(R)-2-benzyl-5-nitro-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.00016
(S)-2-benzyl-5-nitro-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.207
2-benzyl-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0002
2-benzyl-5,5,5-trifluoro-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.015
2-benzyl-5-bromo-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0000000048
(2S)-2-([hydroxy[(1R)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.00000018
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.0000000084
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.000000059
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.000000082
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.000000077
(2S)-2-([hydroxy[(1S)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.0000009
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.00000009
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.0000021
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.0000042
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.0000009
(2S)-2-[(hydroxy[(1R)-1-[(1,4,7,10-tetraazacyclododecan-1-ylacetyl)amino]ethyl]phosphoryl)oxy]-3-phenylpropanoic acid
-
pH 7.5, 25°C
0.19
(2S,3R)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
0.000000015 - 0.00000026
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
0.00529
2-(1-hydroxy-5-oxopyrrolidin-2-yl)-3-phenylpropanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.00259
2-benzyl-3-[(difluoroacetyl)(hydroxy)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.012
2-benzyl-3-[(fluoroacetyl)(hydroxy)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.00139
2-benzyl-3-[formyl(hydroxy)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.009
2-benzyl-3-[hydroxy(methoxyacetyl)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.0994
2-benzyl-3-[hydroxy(methoxycarbonyl)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.00942
2-benzyl-3-[hydroxy(trifluoroacetyl)amino]propanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.00806
3-[acetyl(hydroxy)amino]-2-benzylpropanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.000000026
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1R)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
pH 7.5, 25°C
0.0000032
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1S)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
pH 7.5, 25°C
5.9
threo-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
5.4
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
5.7
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate
0.34
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
1.1
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate
2.2
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
0.000000015
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
pH 7.5, 25°C
0.00000026
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
pH 7.5, 25°C
additional information
additional information
-
D-penicillamine sulfide: Ki-value above 27 mM
-
additional information
additional information
-
residual enzyme activity, 0.2% chitosan hydrochloride 55% activity, 0.2% chitosan citrate 0% activity, 0.04% 8% activity, 0.02% 15% activity, 0.01% 65% activity
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison of activities of enzyme immobilized on different supports, highest activity for polyacrylamide bead support
additional information
-
mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
activity assay, suboptimal condition because chitosan is soluble only until pH 6-6.5
7.5
7.5 - 8
8
-
hydrolysis of protein isolates of Brassica carinata in a batch reactor, trypsin, chymotrypsin, and carboxypeptidase A are used
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
pH-dependent properties of cobalt enzymeûinhibitor complexes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
50
-
hydrolysis of protein isolates of Brassica carinata in a batch reactor, trypsin, chymotrypsin, and carboxypeptidase A are used
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mainly, protein P30, tentatively identified as inactive monomeric carboxypeptidase based on immunoreaction, properties shared with tubulin carboxypeptidase A
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). CBPA1_BOVIN
419
0
47082
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105700
-
biotin-PEG(5000)-carboxypeptidase complex, stoichiometry with avidin 1 : 1, determined by MALDI-TOF
142300
-
biotin-PEG(3400)-carboxypeptidase complex, stoichiometry with avidin 1 : 2, determined by MALDI-TOF
146300
-
biotin-PEG(3400)-carboxypeptidase-PEG(2000) complex, stoichiometry with avidin 1 : 2, determined by MALDI-TOF
233000
-
biotin-PEG(5000)-carboxypeptidase-PEG(2000) complex, stoichiometry with avidin 1 : 4, determined by MALDI-TOF
additional information
additional information
-
molecular weight of trimeric procarboxypeptidase 87000, molecular weight of carboxypeptidase precursor subunit 40000-42000, slight differences in molecular weight may be caused by different activation conditions
additional information
-
molecular weight of trimeric procarboxypeptidase 87000, molecular weight of carboxypeptidase precursor subunit 40000-42000, slight differences in molecular weight may be caused by different activation conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
structure of enzyme and its complex with substrate, overall conformation of the protein, analysis of secondary structures, structure of active center and zinc ligand complex
additional information
-
structure analysis of enzyme in complex with leech carboxypeptidase inhibitor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of enzyme with the inhibitor (S)-N-sulfamoylphenylalaninecrystals are grown by the microdialysis method by equilibrating the protein-inhibitor complex in a solution of 1.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5) against a reservoir containing 0.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5)
crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A
enzyme inhibitor complexes with D-N-hydroxyaminocarbonyl phenylalanine, L-N-hydroxyaminocarbonyl phenylalanine or aminocarbonylphenylalanine
purified enzyme in complex with the tick carboxypeptidase inhibitor, X-ray diffraction structure determination and analysis at 1.7 A resolution, comparison to the structure of unligated enzyme PDB code 1M4L, overview
analysis of enzyme-substrate complex by difference Fourier techniques, analysis of enzyme-inhibitor complexes, mechanistic model based on crystal structure
-
crystal structure of complex with inactivator 2-benzyl-3-iodo-propanoic acid in two crystal forms
-
crystallization reduces catalytic efficiency, abolishes substrate inhibition observed in solution
-
enzyme in complex with leech carboxypeptidase inhibitor, complexing in 50 mM Tris-HCl, pH 7.5, and 100 mM NaCl, at 20°C, complex purification by gel filtration, crystallization by mixing of equal volumes of protein, containing 10-12 mg/ml protein, and reservoir solutions, the latter containing 1.5 M lithium sulfate monohydrate and 100 mM Tris, pH 8.5, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
high-resolution crystallographic studies of enzyme-substrate and enzyme-inhibitor complexes
-
mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
-
structural analysis of enzyme-GlyTyr complexes, design of mechanism-based inactivators based thereon
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
35% activity after 30 min of immobilized enzyme, no activity of soluble enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea influences general stability, 4 M, 0°C, pH 7.5, 24 h, stable, 7 M, 0°C, pH 7.5, 24 h, unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 mg/ml bovine serum albumin and Zn2+ stabilize the washed enzyme crystals from a commercial preparation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of commercial preparation by gel filtration in presence of Zn2+ and latexin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reversible denaturation: up to at least 7 M urea, irreversible: 33% ethanol-water mixture
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is a target for drug development for biotechnological and biomedical applications
analysis
-
the enzyme serves as model enzyme for design of specific inhibiors for zinc proteases
biotechnology
-
multi-block, surfactant copolymers are suitable for applications in which refolding of denaturated or misfolded proteins and suppression of aggregation are important objects
drug development
-
the enzyme serves as model enzyme for design of specific inhibiors for zinc proteases
food industry
medicine
pharmacology
-
construction of synthetic artificial protease with substrate selectivity for CPA as a substrate, designing of the catalyst by use of specific CPA inhibitors, the artificial catalyst can be used as drug with the target being a protein or peptide related to a disease, overview
synthesis
food industry
-
Brassica carinata protein hydrolysates could be used for developing functional foods for the treatment of heart and related diseases
food industry
-
hydrolyzates could be used for preparing special diets when there is a need to increase the supply of branched amino acids and/or reduce the intake of aromatic amino acids
medicine
-
design of mechanism-based, specific inhibitors to cure disease caused by enzyme overfunction
medicine
-
increased activity of carboxypeptidase A has been demonstrated in plasma samples from patients with pancreatitis
medicine
-
the avidin-biotin-PEGylated-carboxypeptidase complex has a great potential as a therapeutic protein delivery system for solid tumor prodrug targeting
synthesis
-
enzymatic modification of human haemoglobin, useful for functional studies
synthesis
-
useful tools for peptide biosynthesis in non-conventional media, considered
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ludwig, M.
Carboxypeptidase A and other peptidases
Inorg. Biochem.
1
438-487
1973
Bos taurus, Squalus acanthias
-
Christianson, D.W.; Lipscomb, D.W.
Carboxypeptidase A
Acc. Chem. Res.
22
62-69
1989
Bos taurus
-
Riordan, J.F.; Holmquist, B.
Carboxypeptidase A
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
44-55
1984
Bos taurus, Homo sapiens
-
Appel, W.
Carboxypeptidasen
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
1023-1037
1974
Bos taurus, Homo sapiens, Rattus norvegicus
-
Petra, P.H.
Bovine procarboxypeptidase and carboxypeptidase A
Methods Enzymol.
19
460-503
1970
Bos taurus
-
Oshima, G.; Nagasawa, K.
Purification of carboxypeptidase A using Sepharose 4B-bound 3-phenylpropionate
J. Biochem.
81
1285-1291
1977
Bos taurus
Spilburg, C.A.; Bethune, J.L.; Vallee, B.L.
Kinetic properties of crystalline enzymes. Carboxypeptidase A
Biochemistry
16
1142-1150
1977
Bos taurus
Reeck, G.R.; Walsh, K.A.; Neurath, H.
Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice
Biochemistry
10
4690-4698
1971
Bos taurus
Petra, P.H.; Neurath, H.
Heterogeneity of bovine carboxypeptidase A. II. Chromatographic purification of carboxypeptidase A (Cox)
Biochemistry
8
5029-5036
1969
Bos taurus
Petra, P.H.; Neurath, H.
The heterogeneity of bovine carboxypeptidase A. I. The chromatographic purification of carboxypeptidase A (Anson)
Biochemistry
8
2466-2475
1969
Bos taurus
Shoham, G.; Rees, D.C.; Lipscomb, W.M.
Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies
Proc. Natl. Acad. Sci. USA
81
7767-7771
1984
Bos taurus
Auld, D.S.; Vallee, B.L.
Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides
Biochemistry
9
602-609
1970
Bos taurus
Lipscomb, W.N.
Relationship of the three-dimensional structure of carboxypeptidase A to catalysis
Tetrahedron
30
1725-1732
1974
Bos taurus
-
Homandberg, G.A.; Peanasky, R.J.
Characterization of proteins from Ascaris lumbricoides which bind specifically to carboxypeptidase
J. Biol. Chem.
251
2226-2233
1976
Bos taurus, Sus scrofa
Birk, Y.
Proteinase inhibitors from potatoes
Methods Enzymol.
45
728-739
1976
Bos taurus
Lipscomb, W.N.
Carboxypeptidase A mechanisms
Proc. Natl. Acad. Sci. USA
77
3875-3878
1980
Bos taurus
Rees, D.C.; Lewis, M.; Honzatko, R.B.; Lipscomb, W.M.; Hardman, K.D.
Zinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution
Proc. Natl. Acad. Sci. USA
78
3408-3412
1981
Bos taurus
Ault, D.S.; Galdes, A.; Geoghegan, K.F.; Holmquist, B.; Martinelli, R.A.; Vallee, B.L.
Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A
Proc. Natl. Acad. Sci. USA
81
5041-5045
1984
Bos taurus
Nowak, E.; Dabrowska, R.
Properties of carboxypeptidase A-treated chicken gizzard tropomyosin
Biochim. Biophys. Acta
829
335-341
1985
Bos taurus
Kilmartin, J.V.
Removal of specific C-terminal residues from human hemoglobin using carboxypeptidases A and B
Methods Enzymol.
76
167-171
1981
Bos taurus
Mock, W.L.; Tsay, J.T.
pK Values for active site residues of carboxypeptidase A
J. Biol. Chem.
263
8635-8641
1988
Bos taurus
Gettins, P.
On the coordination of inhibitors to the metal ion of carboxypeptidase A. A 113Cd and 31P NMR study
J. Biol. Chem.
261
15513-15518
1986
Bos taurus
Suh, J.; Cho, W.; Chung, S.
Carboxypeptidase A-catalysed hydrolysis of alpha-(acylamino)cinnamoyl derivatives of L-beta-phenyllactate and L-phenylalaninate: evidence for acyl-enzyme intermediates
J. Am. Chem. Soc.
107
4530-4535
1985
Bos taurus
-
Lee, K.J.; Kim, D.H.
Design of mechanism-based carboxypeptidase A inactivators on the basis of the X-ray crystal structure and catalytic reaction pathway
Bioorg. Med. Chem.
6
1613-1622
1998
Bos taurus
Vertesi, A.; Simon, L.M.; Kiss, I.; Szajani, B.
Preparation, characterization and application of immobilized carboxypeptidase A
Enzyme Microb. Technol.
25
73-79
1999
Bos taurus
-
Asante-Appiah, E.; Chan, W.C.
Analysis of the interactions between an enzyme and multiple inhibitors using combination plots
Biochem. J.
320
17-26
1996
Bos taurus
Zenchenko, T.A.; Morozov, V.N.
Mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
Protein Sci.
4
251-257
1995
Bos taurus
Mock, W.L.; Wang, L.
Synergistic inhibition of carboxypeptidase A by zinc ion and imidazole
Biochem. Biophys. Res. Commun.
257
239-243
1999
Bos taurus
Weizetfel, J.C.; Smania, A.M.; Barra, H.S.; Argarana, C.E.
A brain protein (P30) that immunoreacts with a polyclonal anti-pancreatic carboxypeptidase A antibody shows properties that are shared with tubulin carboxypeptidase
Mol. Cell. Biochem.
170
139-146
1997
Bos taurus
Banci, L.; Schroeder, S.; Kollman, P.A.
Molecular dynamics characterization of the active cavity of carboxypeptidase A and some of its inhibitor adducts
Proteins
13
288-305
1992
Bos taurus
Chai, J.J.; He, C.H.; Li, M.; Tang, L.; Ming, L.
Crystal structure of carboxypeptidase A complexed with an inactivator in two crystal forms
Protein Eng.
11
841-845
1998
Bos taurus
Zhang, K.; Chance, B.
X-ray absorption fine structure study of the active site of zinc and cobalt carboxypeptidase A in their solution and crystalline forms
Biochemistry
31
1159-1168
1992
Bos taurus
Auld, D.S.; Bertini, I.; Donaire, A.; Messori, L.; Moratal, J.M.
pH-dependent properties of cobalt(II) carboxypeptidase A-inhibitor complexes
Biochemistry
31
3840-3846
1992
Bos taurus
Larsen, K.S.; Auld, D.S.
Carboxypeptidase A: mechanism of zinc inhibition
Biochemistry
28
9620-9625
1989
Bos taurus
Kim, H.; Lipscomb, N.
Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography
Biochemistry
30
8171-8180
1991
Bos taurus
Kilshtain-Vardi, A.; Glick, M.; Greenblatt, H.M.; Goldblum, A.; Shoham, G.
Refined structure of bovine carboxypeptidase A at 1.25 A resolution
Acta Crystallogr. Sect. D
59
323-333
2003
Bos taurus
van Aalten, D.M.F.; Chong, C.R.; Joshua-Tor, L.
Crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75.ANG. - Inhibitor-induced conformational changes
Biochemistry
39
10082-10089
2000
Bos taurus (P00730)
Mock, W.L.; Cheng, H.
Principles of hydroxamate inhibition of metalloproteases: carboxypeptidase A
Biochemistry
39
13945-13952
2000
Bos taurus
Chong, C.R.; Auld, D.S.
Inhibition of carboxypeptidase A by D-penicillamine: mechanism and implications for drug design
Biochemistry
39
7580-7588
2000
Bos taurus
Cho, J.H.; Kim, D.H.; Lee, K.J.; Choi, K.Y.
The role of Tyr248 probed by mutant bovine carboxypeptidase A: insight into the catalytic mechanism of carboxypeptidase A
Biochemistry
40
10197-10203
2001
Bos taurus
Cho, J.H.; Kim, D.H.; Chung, S.J.; Ha, N.C.; Oh, B.H.; Yong Choi, K.
Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A
Bioorg. Med. Chem.
10
2015-2022
2002
Bos taurus (P00730)
Lee, M.; Kim, D.H.
Syntheses and kinetic evaluation of racemic and optically active 2-benzyl-2-methyl-3,4-epoxybutanoic acids as irreversible inactivators for carboxypeptidase A
Bioorg. Med. Chem.
10
913-922
2002
Bos taurus
Jin, J.Y.; Tian, G.R.; Kim, D.H.
Optically active 2-benzyl-3-methanesulfinylpropanoic acid: Synthesis and evaluation as inhibitors for carboxypeptidase A
Bioorg. Med. Chem.
11
4377-4381
2003
Bos taurus
Lee, H.S.; Kim, D.H.
Synthesis and evaluation of alpha,alpha-disubstituted-3-mercaptopropanoic acids as inhibitors for carboxypeptidase A and implications with respect to enzyme inhibitor design
Bioorg. Med. Chem.
11
4685-4691
2003
Bos taurus
Park, J.D.; Kim, D.H.
Sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A
Bioorg. Med. Chem.
12
2349-2356
2004
Bos taurus, Homo sapiens
Lee, M.; Kim, D.H.
Hippuryl-alpha-methylphenylalanine and hippuryl-alpha-methylphenyllactic acid as substrates for carboxypeptidase A. Syntheses, kinetic evaluation and mechanistic implication
Bioorg. Med. Chem.
8
815-823
2000
Bos taurus
Chung, S.J.; Kim, D.H.
N-(Hydroxyaminocarbonyl)phenylalanine: a novel class of inhibitor for carboxypeptidase A
Bioorg. Med. Chem.
9
185-189
2001
Bos taurus
Park, J.D.; Lee, K.J.; Kim, D.H.
A new inhibitor design strategy for carboxypeptidase A as exemplified by N-(2-chloroethyl)-N-methylphenylalanine
Bioorg. Med. Chem.
9
237-243
2001
Bos taurus
Marino-Buslje, C.; Venhudova, G.; Molina, M.A.; Oliva, B.; Jorba, X.; Canals, F.; Aviles, F.X.; Querol, E.
Contribution of C-tail residues of potato carboxypeptidase inhibitor to the binding to carboxypeptidase A A mutagenesis analysis
Eur. J. Biochem.
267
1502-1509
2000
Bos taurus
Park, J.D.; Kim, D.H.; Kim, S.J.; Woo, J.R.; Ryu, S.E.
Sulfamide-based inhibitors for carboxypeptidase A. Novel type transition state analogue inhibitors for zinc proteases
J. Med. Chem.
45
5295-5302
2002
Bos taurus (P00730)
Park, J.D.; Kim, D.H.
Cysteine derivatives as inhibitors for carboxypeptidase A: synthesis and structure-activity relationships
J. Med. Chem.
45
911-918
2002
Bos taurus
Chung, S.J.; Chung, S.; Lee, H.S.; Kim, E.J.; Oh, K.S.; Choi, H.S.; Kim, K.S.; Kim, Y.J.; Hahn, J.H.; Kim, D.H.
Mechanistic insight into the inactivation of carboxypeptidase A by alpha-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid, a novel type of irreversible inhibitor for carboxypeptidase A with no stereospecificity
J. Org. Chem.
66
6462-6471
2001
Bos taurus
Arolas, J.L.; Lorenzo, J.; Rovira, A.; Vendrell, J.; Aviles, F.X.; Ventura, S.
Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties
Biochemistry
43
7973-7982
2004
Bos taurus
Song, J.B.; Hah, S.S.; Suh, J.
Cyclen-containing inhibitors of carboxypeptidase A synthesized in search of target-selective artificial proteases
Bull. Korean Chem. Soc.
25
1703-1706
2004
Bos taurus
-
Kim, D.H.
Chemistry-based design of inhibitors for carboxypeptidase A
Curr. Top. Med. Chem.
4
1217-1226
2004
Bos taurus
Arolas, J.L.; Popowicz, G.M.; Lorenzo, J.; Sommerhoff, C.P.; Huber, R.; Aviles, F.X.; Holak, T.A.
The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
J. Mol. Biol.
350
489-498
2005
Bos taurus (P00730), Bos taurus
Arolas, J.L.; Popowicz, G.M.; Bronsoms, S.; Aviles, F.X.; Huber, R.; Holak, T.A.; Ventura, S.
Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond
J. Mol. Biol.
352
961-975
2005
Bos taurus
Phoon, L.; Burton, N.A.
Assessment of a mechanism for reactive inhibition of carboxypeptidase A with QM/MM methods
J. Mol. Graph. Model.
24
94-101
2005
Bos taurus
Mouradov, D.; Craven, A.; Forwood, J.K.; Flanagan, J.U.; Garcia-Castellanos, R.; Gomis-Rueth, F.X.; Hume, D.A.; Martin, J.L.; Kobe, B.; Huber, T.
Modelling the structure of latexin-carboxypeptidase A complex based on chemical cross-linking and molecular docking
Protein Eng. Des. Sel.
19
9-16
2006
Bos taurus (P00730)
Hennig, A.; Florea, M.; Roth, D.; Enderle, T.; Nau, W.M.
Design of peptide substrates for nanosecond time-resolved fluorescence assays of proteases: 2,3-Diazabicyclo[2.2.2]oct-2-ene as a noninvasive fluorophore
Anal. Biochem.
360
255-265
2007
Bos taurus
Mustafi, D.; Smith, C.M.; Makinen, M.W.; Lee, R.C.
Multi-block poloxamer surfactants suppress aggregation of denatured proteins
Biochim. Biophys. Acta
1780
7-15
2008
Bos taurus
Ke, S.; Wright, J.C.; Kwon, G.S.
Avidin-biotin-PEG-CPA complexes as potential EPR-directed therapeutic protein carriers: preparation and characterization
Bioconjug. Chem.
18
1644-1650
2007
Bos taurus
Schmidt, D.; Brennan, S.O.
Modified form of the fibrinogen Bbeta chain (des-Gln Bbeta), a potential long-lived marker of pancreatitis
Clin. Chem.
53
2105-2111
2007
Bos taurus
Bonferoni, M.C.; Sandri, G.; Rossi, S.; Ferrari, F.; Gibin, S.; Caramella, C.
Chitosan citrate as multifunctional polymer for vaginal delivery. Evaluation of penetration enhancement and peptidase inhibition properties
Eur. J. Pharm. Sci.
33
166-176
2008
Bos taurus, Sus scrofa
Pedroche, J.; Yust, M.M.; Lqari, H.; Megias, C.; Giron-Calle, J.; Alaiz, M.; Vioque, J.; Millan, F.
Obtaining of Brassica carinata protein hydrolysates enriched in bioactive peptides using immobilized digestive proteases
Food Res. Int.
40
931-938
2007
Bos taurus
Pedroche, J.; Yust, M.d.e.l.M.; Lqari, H.; Megias, C.; Giron-Calle, J.; Alaiz, M.; Vioque, J.; Millan, F.
Production of Brassica carinata protein hydrolyzates with a high Fischers ratio using immobilized proteases
J. Agric. Food Chem.
54
7621-7627
2006
Bos taurus
Yanes, O.; Aviles, F.X.; Roepstorff, P.; J?rgensen, T.J.
Exploring the "intensity fading" phenomenon in the study of noncovalent interactions by MALDI-TOF mass spectrometry
J. Am. Soc. Mass Spectrom.
18
359-367
2007
Bos taurus
Chong, C.R.; Auld, D.S.
Catalysis of zinc transfer by D-penicillamine to secondary chelators
J. Med. Chem.
50
5524-5527
2007
Bos taurus
Cowieson, N.P.; Miles, A.J.; Robin, G.; Forwood, J.K.; Kobe, B.; Martin, J.L.; Wallace, B.A.
Evaluating protein:protein complex formation using synchrotron radiation circular dichroism spectroscopy
Proteins
70
1142-1146
2008
Bos taurus
Masuhara, M.; Sato, T.; Hada, N.; Hakeda, Y.
Protective protein/cathepsin A down-regulates osteoclastogenesis by associating with and degrading NF-kappaB p50/p65
J. Bone Miner. Metab.
27
46-56
2009
Bos taurus
Wang, S.F.; Tian, G.R.; Zhang, W.Z.; Jin, J.Y.
Characterization of alpha-nitromethyl ketone as a new zinc-binding group based on structural analysis of its complex with carboxypeptidase A
Bioorg. Med. Chem. Lett.
19
5009-5011
2009
Bos taurus (P00730)
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