3.4.17.1: carboxypeptidase A
This is an abbreviated version!
For detailed information about carboxypeptidase A, go to the full flat file.
Word Map on EC 3.4.17.1
-
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
- 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
Reaction
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro =
Synonyms
A-type metallocarboxypeptidase, AcCP, Anson's enzyme, ASPA, aspartoacyclase, carboxypeptidase, carboxypeptidase a, carboxypeptidase A-6, carboxypeptidase A-like activity, carboxypeptidase A1, carboxypeptidase A2, Carboxypeptidase A3, carboxypeptidase A4, carboxypeptidase vitellogenic-like, carboxypeptidase-A, carboxypolypeptidase, colon mast cell carboxypeptidase, CPA, CPA1, CPA3, CPA4, CPA6, CPAI, CPD, CPVL, EC 3.4.12.2, EC 3.4.2.1, hCPA, hCPA4, mast cell carboxypeptidase A, mast cell CPA, mast cell-CPA, mast-cell carboxypeptidase A, mast-cell CPA, MC-CP, MC-CPA, MCCPA, MCP-2, mCPA, MDCP-A1, MDCP-A2, MeCPA, MF-CPA, molting carboxypeptidase A, molting fluid carboxypeptidase A, More, Nna1/CCP1, ochratoxin A hydrolytic enzyme, PTD012, RMC-CP, vitellogenic-like carboxypeptidase
ECTree
3.4.17.1 carboxypeptidase AAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.17.1 - carboxypeptidase A
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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
3-(2-furyl)acryloyl-L-Phe-L-Ala + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ala
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Ile + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ile
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Leu + H2O
3-(2-furyl)acryloyl-L-Phe + L-Leu
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Met + H2O
3-(2-furyl)acryloyl-L-Phe + L-Met
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Phe + H2O
3-(2-furyl)acryloyl-L-Phe + L-Phe
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Trp + H2O
3-(2-furyl)acryloyl-L-Phe + L-Trp
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Val + H2O
3-(2-furyl)acryloyl-L-Phe + L-Val
-
-
-
-
?
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
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + ?
-
-
-
ir
carbobenzyloxy-Gly-hippuryl-L-Phe + H2O
carbobenzyloxy-Gly-hippuric acid + L-Phe
-
-
-
ir
carboxypeptidase A5 C-terminus + H2O
?
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
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-DL-beta-phenylacetic acid + H2O
hippuric acid + DL-phenylacetic acid
-
-
-
-
?
hippuryl-DL-beta-phenyllactic acid + H2O
hippuric acid + 3-phenyllactic acid
-
-
-
ir
hippuryl-DL-phenylalanine + H2O
hippuric acid + DL-phenylalanine
-
-
-
-
?
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
-
-
?
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
Met-enkephalin + H2O
?
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
-
low activity
-
-
?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
-
high activity
-
-
?
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-(3-[2-furyl]acryloyl)-L-Phe-L-Phe + H2O
N-(3-[2-furyl]acryloyl)-L-Phe + L-Phe
-
-
-
-
?
N-(3-[2-furyl]acryloyl)-Phe-Phe + H2O
?
substrate of carboxypeptidase activity assay
-
-
?
N-(3-[2-furyl]acryloyl)-Phe-Phe + H2O
N-(3-[2-furyl]acryloyl)-Phe + Phe
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe-OH + H2O
?
-
substrate for inhibition assay
-
-
?
N-(trans-3-indoleacryloyl)-L-Phe + H2O
trans-3-indoleacrylate + L-Phe
-
-
-
ir
N-acetyl-Gly-L-phenyllactic acid + H2O
N-acetyl-Gly + L-phenyllactic acid
-
-
-
ir
N-carbobenzoxy-Gly-Gly-L-Leu + H2O
N-carbobenzoxy-Gly-Gly + L-Leu
-
-
-
ir
N-carbobenzoxy-Gly-Gly-L-Phe + H2O
N-carbobenzoxy-Gly-Gly + 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
-
-
?
O-(trans-4-chlorocinnamoyl)-L-beta-phenyllactate + H2O
trans-4-chlorocinnamic acid + L-phenyllactic acid
-
-
-
?
O-(trans-4-chlorocinnamoyl)-L-phenyllactic acid + H2O
trans-4-chlorocinnamic acid + L-phenyllactic 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
-
-
?
Phe-Asn-Arg-Pro-Val + H2O
?
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Asp + H2O
?
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Val + H2O
?
used as substrate in the activity assay
-
-
?
voltage-dependent anion channel protein 1 C-terminus + H2O
?
-
weak substrate
-
-
?
angiotensin I + H2O
?
-
partial cleavage of about 50% of angiotensin is found after 30 min of incubation with CPA4
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
ir
hippuryl-DL-phenyllactic acid + H2O
hippuric acid + DL-phenyllactic acid
-
-
-
-
?
hippuryl-DL-phenyllactic acid + H2O
hippuric acid + DL-phenyllactic acid
-
-
-
ir
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
assay substrate
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
-
-
-
?
hippuryl-L-phenyllactate + H2O
hippuric acid + L-phenyllactate
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
-
prodrug activation in SW122 cells
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
-
-
-
-
?
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
-
-
?
additional information
?
-
the enzyme is a secretory granule metalloexopeptidase, MC-CPA is unique among carboxypeptidases inthaving a CPA-like substrate-binding pocket and enzymatic activity despite overall protein and gene structures more similar to CPB
-
-
?
additional information
?
-
-
the enzyme is a secretory granule metalloexopeptidase, MC-CPA is unique among carboxypeptidases inthaving a CPA-like substrate-binding pocket and enzymatic activity despite overall protein and gene structures more similar to CPB
-
-
?
additional information
?
-
-
CPVL colocalizes with both macrophage-inhibitory protein-1alpha and tumour necrosis factor-alpha
-
-
?
additional information
?
-
-
CPA4 is able to cleave hydrophobic C-terminal residues with a preference for Phe, Leu, Ile, Met, Tyr, and Val. Aliphatic, aromatic, and basic residues in the P1 position have a positive influence on the cleavage specificity. In contrast, acidic residues, Pro, and Gly have a negative influence in the P1 position
-
-
?
additional information
?
-
-
neither bradykinin nor des-Arg9-bradykinin or 3-(2-furyl)acryloyl-L-Phe-L-His are substrates for CPA4
-
-
?
additional information
?
-
-
the enzyme cleaves C-terminal hydrophobic aliphatic and aromatic residues from other peptides and proteins, not of food in contrast to pancreatic CPA1 and CPA2, for destruction, presumably following the action of chymase
-
-
?
