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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
-
36317, 36319, 36322, 36341, 36344, 36345, 36346, 36349, 36352, 36353, 36356, 36361
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
relationships between enzyme structure and catalytic properties, catalytic groups, intermediates, and conformational changes during catalysis conform to "induced fit hypothesis"
-
-
-
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
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
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
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(Ala)4 + H2O
(Ala)3 + L-Ala
-
-
-
ir
(S)-hippuryl-alpha-MePhe + H2O
?
-
-
-
?
(S)-hippuryl-alpha-methylphenyllactic acid + H2O
?
-
-
-
?
(S)-hippuryl-OPhe + H2O
?
-
-
-
?
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
Ac-Phe-ThiaPhe + H2O
Phe + ThiaPhe
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + Leu
-
-
-
ir
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
anisylazoformyl-L-Phe + H2O
anisylazoformic acid + L-Phe
-
-
-
?
apolipoprotein B + H2O
?
-
-
-
-
?
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + ?
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
?
-
-
-
-
?
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
benzoyl-Gly-phenyllactate + H2O
benzoyl-Gly-phenyllactate + ?
-
-
-
ir
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
-
-
-
ir
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
-
-
ir
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
ir
beta-actin (169-177) + H2O
?
-
weak substrate
-
-
?
big SAAS + H2O
?
-
good substrate
-
-
?
carbobenzoxy-Gly-Gly-L-Tyr + H2O
carbobenzoxy-Gly-Gly + L-Tyr
-
-
-
ir
carbobenzoxy-Gly-Gly-Leu + H2O
carbobenzoxy-Gly-Gly + Leu
-
-
-
ir
carbobenzoxy-Gly-Gly-Phe + H2O
carbobenzoxy-Gly-Gly + Phe
-
-
-
ir
carbobenzoxy-Gly-Gly-Val + H2O
carbobenzoxy-Gly-Gly + Val
-
-
-
ir
carbobenzoxy-Gly-L-Leu + H2O
carbobenzoxy-Gly + L-Leu
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
carbobenzoxy-Gly-L-Trp + H2O
carbobenzoxy-Gly + L-Trp
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
-
-
?
cathepsin D (138-155) + H2O
?
-
weak substrate
-
-
?
chromogranin A (374-388) + H2O
?
-
good substrate
-
-
?
chromogranin A (374-390) + H2O
?
-
weak substrate
-
-
?
chromogranin B + H2O
?
-
good substrate
-
-
?
cinnamoyl-L-phenyllactate + H2O
cinnamic acid + L-phenyllactate
-
-
-
ir
clathrin light chain A C-terminus + H2O
?
-
weak substrate
-
-
?
dansylglycylglycyl-L-tryptophan + H2O
?
-
assay substrate
-
-
?
des-Asp1-angiotensin + H2O
?
-
partially cleaved in 2 h
-
-
?
dynorphin A8 + H2O
?
-
weak substrate
-
-
?
elongation factor 1 beta 2 N-terminus + H2O
?
-
good substrate
-
-
?
endothelin + H2O
?
-
removal of the C-terminal tryptophan
-
-
?
endothelin-1 + H2O
?
-
-
-
-
?
gamma-actin + H2O
?
-
weak substrate
-
-
?
Gly-L-Tyr + H2O
Gly + L-Tyr
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-phenyllactate + H2O
?
-
-
-
?
hippuryl-DL-beta-phenyllactic acid + H2O
hippuric acid + 3-phenyllactic acid
-
-
-
ir
hippuryl-DL-phenylalanine + H2O
hippuric acid + DL-phenylalanine
-
-
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
hippuryl-DL-phenyllactic acid + H2O
hippuric acid + DL-phenyllactic acid
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
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
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + Phe
hippuryl-L-phenylalanine + H2O
?
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
hippuryl-L-phenyllactate + H2O
hippuric acid + L-phenyllactate
hippuryl-Phe + H2O
hippuric acid + Phe
kinetensin + H2O
?
-
-
-
-
?
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
Leu-enkephalin + H2O
?
-
partially cleaved in 2 h
-
-
?
little SAAS + H2O
?
-
small percentage of cleavage
-
-
?
Met-enkephalin + H2O
?
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
Met-enkephalin-L-Arg-L-Phe + H2O
Met-enkephalin-L-Arg + L-Phe
-
-
-
-
?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
-
low activity
-
-
?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
-
high activity
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
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-(2-furanacryloyl)-Phe-Phe + H2O
N-(2-furanacryloyl)-Phe + Phe
-
-
-
ir
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
?
-
-
-
?
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-methoxyphenyl-azoformyl)-L-Phe + H2O
?
-
-
-
?
N-(4-methoxyphenylazoformyl)-L-phenylalanine + H2O
?
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe + H2O
?
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe-OH + H2O
?
-
substrate for inhibition assay
-
-
?
N-(methoxyphenyl-azoformyl)-Phe-OH + H2O
?
-
-
-
-
?
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-acetyl-L-aspartate
acetate + L-aspartate
-
-
-
-
?
N-acetyl-phenylalanyl-L-3-thiaphenylalanine + H2O
?
-
assay substrate
-
-
?
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-carbobenzoxy-Gly-L-Phe + H2O
N-carbobenzoxy-Gly + L-Phe
-
-
-
ir
N-carbobenzoxy-Gly-L-Tyr + H2O
N-carbobenzoxy-Gly + L-Tyr
-
-
-
ir
N-[3-(2-furyl)acryloyl]-Phe-Phe + H2O
?
-
-
-
-
?
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
-
-
-
?
N-[4-methoxyphenylazoformyl]-Phe-OH + H2O
?
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
-
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
O-(trans-p-chlorocinnamoyl)-L-phenylacetic acid + H2O
?
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-phenyllactic acid + H2O
?
-
-
?
O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate + H2O
?
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
p-nitrophenyl acetate + H2O
nitrophenolate + acetate
-
-
-
-
?
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
-
-
?
peptidylprolyl isomerase A (118-129) + H2O
?
-
good substrate
-
-
?
peptidylprolyl isomerase A (23-39) + H2O
?
-
weak substrate
-
-
?
peptidylprolyl isomerase A (26-39) + H2O
?
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-100) + H2O
?
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-92) + H2O
?
-
weak substrate
-
-
?
peroxiredoxin V N-terminus + H2O
?
-
good substrate
-
-
?
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
-
-
?
procholecystokinin (46-62) + H2O
?
-
weak substrate
-
-
?
procholecystokinin (46-63) + H2O
?
-
weak substrate
-
-
?
proenkenphalin octapeptide + H2O
?
-
weak substrate
-
-
?
proenkephalin + H2O
?
-
good substrate
-
-
?
propeptidyl-amidating monooxygenase + H2O
?
-
good substrate
-
-
?
proteasome subunit beta type 6 (34-41) + H2O
?
-
weak substrate
-
-
?
protein PEN + H2O
?
-
good substrate
-
-
?
protein PEN-20 + H2O
?
-
good substrate
-
-
?
provasopressin (151-end) + H2O
?
-
weak substrate
-
-
?
ribosomal protein S21 C-terminus + H2O
?
-
weak substrate
-
-
?
secretogranin (287-316) + H2O
?
-
weak substrate
-
-
?
secretogranin (300-316) + H2O
?
-
weak substrate
-
-
?
snake venom toxin + H2O
?
-
-
-
-
?
synaptosomal-associated protein C-terminus + H2O
?
-
good substrate
-
-
?
thioredoxin N-terminus + H2O
?
-
weak substrate
-
-
?
vacuolar ATP synthase subunit 2 C-terminus + H2O
?
-
weak substrate
-
-
?
vasoconstrictive factor endothelin 1 + H2O
?
-
-
-
-
?
voltage-dependent anion channel protein 1 C-terminus + H2O
?
-
weak substrate
-
-
?
xenopsin + H2O
?
-
-
-
-
?
additional information
?
-
alpha-tubulin + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
-
-
-
?
angiotensin I + H2O
?
-
-
-
-
?
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
-
-
?
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
-
-
-
-
?
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
-
-
-
-
?
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
-
-
-
-
?
apoB-100 + H2O
?
-
-
-
-
?
apoB-100 + H2O
?
-
-
-
-
?
apoB-100 + H2O
?
-
-
-
-
?
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Leu + H2O
carbobenzoxy-Gly + L-Leu
-
-
-
ir
carbobenzoxy-Gly-L-Leu + H2O
carbobenzoxy-Gly + L-Leu
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
-
-
-
ir
carbobenzoxy-Gly-L-Trp + H2O
carbobenzoxy-Gly + L-Trp
-
-
-
ir
carbobenzoxy-Gly-L-Trp + H2O
carbobenzoxy-Gly + L-Trp
-
-
-
ir
ET-1 + H2O
?
-
-
-
-
?
Gly-L-Tyr + H2O
Gly + L-Tyr
-
-
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
-
low activity
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
-
low activity
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
-
slow substrate
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
-
-
-
-
?
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-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-Phe + H2O
hippuric acid + L-Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + Phe
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + Phe
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
assay substrate
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
-
-
-
?
hippuryl-L-phenyllactate + H2O
hippuric acid + L-phenyllactate
-
-
-
-
?
hippuryl-L-phenyllactate + H2O
hippuric acid + L-phenyllactate
-
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
-
-
-
?
Leu5-enkephalin + H2O
?
-
-
-
-
?
Leu5-enkephalin + H2O
?
-
-
-
-
?
Leu5-enkephalin + H2O
?
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
-
prodrug activation in SW122 cells
-
-
?
N-[4-methoxyphenylazoformyl]-Phe-OH + H2O
?
-
-
-
-
?
N-[4-methoxyphenylazoformyl]-Phe-OH + H2O
?
-
assay substrate
-
-
?
neuromedin N + H2O
?
-
-
-
-
?
neuromedin N + H2O
?
-
good substrate
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
-
-
-
-
?
sarafotoxin + H2O
?
-
-
-
-
?
sarafotoxin + H2O
?
-
-
-
-
?
sarafotoxin + H2O
?
-
removal of the C-terminal tryptophan
-
-
?
sarafotoxin + H2O
?
-
-
-
-
?
sarafotoxin 6b + H2O
?
-
-
-
-
?
sarafotoxin 6b + H2O
?
-
-
-
-
?
additional information
?
-
-
human haemoglobin, removal of specific C-terminal residues
-
-
?
additional information
?
-
-
intermediates of biochemical reaction
-
-
?
additional information
?
-
-
chicken gizzard tropomyosin, effects on interaction between tropomyosin and actomyosin ATPase
-
-
?
additional information
?
-
-
acyl-enzyme intermediates
-
-
?
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 acts as a monocarboxypeptidase
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme cleaves dipeptides or single amino acids from the C-terminus of polypeptides
-
-
?
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(+-)-2-benzylsuccinic acid
-
-
(2E)-2-mercapto-3-phenylacrylic acid
-
-
(2E)-2-mercapto-4-phenylbut-2-enoic acid
-
-
(2E)-2-mercapto-5-phenylpent-2-enoic acid
-
-
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
-
(2R,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(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
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
(2S,3R)-2-benzyl-3,4-epoxybutanoic acid
-
-
(2S,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(2S,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(R)-2-benzyl-3-(4-methoxybenzoyl)propanoic acid
-
a ketoester substrate analogue
(R)-2-benzyl-3-(methylthio)propanoic acid
-
-
(R)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
(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
(R)-2-benzyl-5-nitro-4-oxopentanoic acid
-
(R)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
-
(R)-hippuryl-alpha-MePhe
-
-
(R)-N-(2-chloroethyl)-N-methylphenylalanine
-
-
(R)-N-(N-hydroxysulfamoyl)phenylalanine
(R)-N-cyclohexylcysteine
-
-
(R)-N-formyl-N-hydroxyphenylalanine
-
-
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
(R)-N-isopropylcysteine
-
-
(R)-N-phenethylcysteine
-
-
(R)-N-sulfamoylphenylalanine
(R,S)-3-phenyl-2-sulfamoyloxypropionic acid
-
competitive
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
competitive
(R,S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R,S)-N-sulfamoylphenylalanine
-
competitive
(RS)-2-benzyl-3-(methylthio)propanoic acid
-
-
(RS)-2-benzyl-3-nitropropanoic acid
-
-
(RS)-2-benzyl-3-sulfamoylpropionic acid
-
-
(RS)-2-isobutyl-3-nitropropanoic acid
-
-
(RS)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
-
(RS)-2-mercaptomethyl-2-methylbutanoic acid
-
-
(RS)-2-mercaptomethylbutyric acid
-
-
(RS)-3-phenyl-2-sulfamoyloxypropionic acid
-
competitive
(RS)-N-(hydroxyaminocarbonyl)-phenylalanine
-
-
(RS)-N-formyl-N-hydroxyphenylalanine
-
-
(RS)-N-sulfamoylphenylalanine
-
-
(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; i.e. IIle2
(S)-2-benzyl-3-(methylthio)propanoic acid
-
-
(S)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
(S)-2-benzyl-3-nitropropanoic acid
-
-
(S)-2-benzyl-5-nitro-4-oxopentanoic acid
-
(S)-N-(2-chloroethyl)-N-methylphenylalanine
-
-
(S)-N-(N-benzylsulfamoyl)phenylalanine
-
(S)-N-(N-hydroxysulfamoyl)phenylalanine
(S)-N-(N-isopropylsulfamoyl)phenylalanine
-
(S)-N-(N-methylsulfamoiyl)phenylalanine
-
(S)-N-(N-phenylethylsulfamoyl)phenylalanine
-
(S)-N-cyclohexylcysteine
-
-
(S)-N-formyl-N-hydroxyphenylalanine
-
-
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
(S)-N-isopropylcysteine
-
-
(S)-N-methyl-N-sulfamoylphenylalanine
-
(S)-N-phenethylcysteine
-
-
(S)-N-sulfamoylphenylalanine
(S)-N-sulfamoylphenylalanine benzyl ester
pH 7.5
2-(1-Carboxy-2-phenyl ethyl)-4,6-dichlorophenol
-
-
2-(1-Carboxy-2-phenylethyl)-4-phenylazophenol
-
-
2-(1-Carboxy-2-phenylethyl)phenol
-
-
2-(1-hydroxy-5-oxopyrrolidin-2-yl)-3-phenylpropanoic acid
-
-
2-benzyl-3,4-epithiobutanoic acid
-
-
2-benzyl-3,4-epoxybutanoic acid
-
-
2-benzyl-3-iodo-propanoic acid
-
mechanisms elucidated from complex with inactivator
2-benzyl-3-mecaptopropionate
-
Ki: 11 nM
2-benzyl-3-[(difluoroacetyl)(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[(fluoroacetyl)(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[formyl(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(methoxyacetyl)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(methoxycarbonyl)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(trifluoroacetyl)amino]propanoic acid
-
-
2-benzyl-4-oxopentanoic acid
-
2-benzyl-5,5,5-trifluoro-4-oxopentanoic acid
-
2-benzyl-5-bromo-4-oxopentanoic acid
-
2-benzylsuccinic acid
potent inhibitor
3-hydroxyaminocarbonyl-2-benzylpropanoic acid
-
-
3-[acetyl(hydroxy)amino]-2-benzylpropanoic acid
-
-
4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid
mechanism-based inhibitor
4-phenylbutyric acid
-
Ki: 0.118 mM
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
alpha-benzyl-2-oxo-1,3-oxazolidine-5-acetic acid
-
irreversible
aminobenzylsuccinic acid
-
Ki: 0.039 mM
anilino(mercapto)acetic acid
-
-
Ascaris carboxypeptidase inhibitor
-
-
-
CBZ-Ala-Gly-PSI[P(O2)O]-Phe
-
crystallographic study of structure Ki: 0.710 nM
CBZ-Phe-Val-PSI[P(O2)O]-Phe
-
crystallographic study of structure Ki: 0.000011 nM
CdCl2
-
55% inhibition at 1 mM
Co(II)-cyclen complex
-
-
Cu(II)-cyclen complex
-
-
CuCl2
-
complete inhibition at 1 mM
D-N-(hydroxyaminocarbonyl)phenylalanine
-
-
D-N-hydroxyaminocarbonyl phenylalanine
-
DL-benzylsuccinic acid
-
-
DTT
-
52% inhibition at 1 mM
endoglycosidase H
-
lowers CPVL expression in monocyte-derived macrophages
-
Gly-Asn-Arg-Pro-Val-Thr
-
HgCl2
-
80% inhibition at 10 mM
hydroxyalkylphosphinyl L-beta-phenyllactate ester
-
binds to the active site
Hydroxyquinoline sulfonate
imidazole
-
Zn2+ enhances kinetic inhibition by imidazole 560fold due to formation of ternary complexes with enzyme
L-beta-Phenyllactate
-
product inhibition
L-Lys-L-tyrosineamide
-
-
L-N-(aminocarbonyl)phenylalanine
-
-
L-N-(hydroxyaminocarbonyl)phenylalanine
-
-
L-N-hydroxyaminocarbonyl phenylalanine
-
L-Phe-phosphoramidate-phenylester
-
Ki: 0.0021 mM
L-Phenyllactate
-
Ki: 0.058 mM
leech carboxypeptidase inhibitor
-
mercapto(methylamino)acetic acid
-
-
mercaptoacetyl-D-Phe
-
Ki: 220 nM
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
N-(3-chloropropionyl)-L-phenylalanine
-
-
N-(hydroxyacetyl)-Phe
-
irreversible inactivation, Kinact/Ki: 71 M-1s-1
N-Bromoacetyl-N-methyl-L-phenylalanine
-
rapid inactivation
N-glycosidase
-
lowers CPVL expression in monocyte-derived macrophages
-
N-phenylphosphoryl-L-phenylalanine
-
Ki: 0.0021 mM
O-(hydroxyacetyl)-beta-phenyllactate
-
irreversible inactivation, Kinact/Ki: 57 M-1s-1
o-phenanthroline
1 mM strongly inhibits
O-[[(1R)-(N-phenylmethoxycarbonyl)-L-alanyl]aminoethyl]hydroxyphosphinyl-L-3-phenyllactate
-
p-iodo-beta-phenylpropionate
-
-
p-nitrophenylacetic acid
-
Ki: 2.5 mM
Phe phosphonate
-
Ki: 0.001 mM
Phe-Asn-Arg-Ala-Val-Asp
-
Phe-Asn-Arg-Ala-Val-Val
-
Phe-Asn-Arg-Pro-Val-Asp
-
Phe-Asn-Arg-Pro-Val-Val
-
polypeptide inhibitor
-
molecular weight 10000, Ki: 1 nM
-
potato carboxypeptidase inhibitor
-
potato carboxypeptidase inhibitor mutant DELTA37-39
-
-
-
potato carboxypeptidase inhibitor mutant DELTA38-39
-
-
-
potato carboxypeptidase inhibitor mutant DELTA39
-
-
-
potato carboxypeptidase inhibitor mutant G39F
-
-
-
potato carboxypeptidase inhibitor mutant P36G
-
-
-
potato carboxypeptidase inhibitor mutant V38G
-
-
-
potato carboxypeptidase inhibitor mutant Y37F
-
-
-
potato carboxypeptidase inhibitor mutant Y37G
-
-
-
potato tuber carboxypeptidase inhibitor
-
95% inhibition at 0.001 mM
-
Proteins from Ascaris lumbricoides
-
molecular weight 7600, Ki in nM range, extensive structural analysis of inhibitors
-
rac-2-(mercaptomethyl)-3-cyclohexylpropanoic acid
-
-
rac-2-(mercaptomethyl)-4-methylpentanoic acid
-
-
rac-2-(mercaptomethyl)-6-phenylhexanoic acid
-
-
rac-2-benzyl-3-mercaptopropanoic acid
-
-
rac-2-benzyl-5-chloropentanoic acid
-
-
rac-N-(1-naphthylmethyl)cysteine
-
-
rac-N-(aminocarbonyl)phenylalanine
-
-
rac-N-(cyclohexylmethyl)cysteine
-
-
rac-N-(hydroxyaminocarbonyl)phenylalanine
-
-
rac-N-(p-methoxy)benzylcysteine
-
-
rac-N-benzyl-N-methylcysteine
-
-
rac-N-cyclohexylcysteine
-
-
rac-N-isobutylcysteine
-
-
rac-N-isopropylcysteine
-
-
rac-N-phenethylcysteine
-
-
rac-N-phenylpropylcysteine
-
-
threo-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
tick carboxypeptidase inhibitor
-
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(R)-N-sulfamoylphenylalanine
-
-
(R)-N-sulfamoylphenylalanine
-
(R)-N-sulfamoylphenylalanine
-
competitive
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(S)-N-sulfamoylphenylalanine
-
-
(S)-N-sulfamoylphenylalanine
-
competitive
1,10-phenanthroline
-
-
1,10-phenanthroline
-
complete inhibition at 1 mM
1,10-phenanthroline
-
80% inhibition at 0.1 mM
1,10-phenanthroline
-
complete inhibition at 10 mM
3-Phenylpropionic acid
-
Ki: 0.062-0.19 mM
3-Phenylpropionic acid
-
Ki: 0.062 mM
3-Phenylpropionic acid
-
84% inhibition at 1 mM, some derivatives also inhibitory
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
noncompetitive, Ki: 0.12 mM
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
Ki: 0.81 mM, noncompetitive
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
Ki: 6.1 mM
3-Phenylpropionic acid
-
Ki: 0.482 mM
Benzylsuccinic acid
-
Ki: 450 nM
Benzylsuccinic acid
-
Ki: 0.0016
Carbobenzoxyglycine
-
-
Carbobenzoxyglycine
-
activator of dipeptide hydrolysis, inhibitor of tripeptide hydrolysis, Ki: 27 mM
Cd2+
-
decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
Cd2+
-
about 30% inhibition in small intestine in vivo
Chelating agents
-
-
chitosan citrate
-
-
chitosan hydrochloride
-
-
chitosan hydrochloride
-
-
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
D-penicillamine
-
-
D-penicillamine
-
catalyzes Zn2+ transfer from carboxypeptidase A to chelators, catalytic chelation
D-Phe
-
Ki: 2 mM
EDTA
-
10 mM
EDTA
-
86% inhibition at 1 mM
EDTA
-
complete inhibition of CPA4 activity s only achieved using a 100 mM concentration of EDTA in an overnight incubation, whereas the same inhibitor concentration causes only 60% inhibition after 5 h of treatment
EDTA
-
complete inhibition at 10 mM
EDTA
10 mM strongly inhibits
Gly-L-Tyr
-
-
Hydroxyquinoline sulfonate
-
-
Hydroxyquinoline sulfonate
-
-
indole acetic acid
-
Ki: 0.078 mM
indole acetic acid
-
noncompetitive, Ki: 0.17 mM
latexin
from mouse recombinantly expressed as His-tagged enzyme in Escherichia coli and purified, overview, analysis of complex formation with CPAI, overview
-
latexin
-
cloned from human brain and expressed in Escherichia coli, CPA4-latexin complex structure determination and analysis
-
latexin
-
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; a carboxypeptidase A inhibitor protein, inhibits mast-cell CPA, CPA1, and CPA2, is associated with intracellular granular structures distinct from MCCPA- and histamine-containing secretory granules and lysosomes in peritoneal mast cells, purification from and expression analysis in peritoneal mast cell granules, overview
-
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
-
leech carboxypeptidase inhibitor
-
LCI
-
leech carboxypeptidase inhibitor
-
-
-
phenylacetic acid
-
Ki: 0.39 mM
phenylacetic acid
-
noncompetitive, Ki: 0.73 mM
potato carboxypeptidase inhibitor
-
molecular weight 38000, detailed study of inhibitor effects, stability, physical properties, purification protocol
-
potato carboxypeptidase inhibitor
-
Ki: 5 nM
-
potato carboxypeptidase inhibitor
-
-
-
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
-
potato carboxypeptidase inhibitor
-
PCI
-
potato carboxypeptidase inhibitor
-
PCI
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
Ki: 2 nM
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
Ki: 107 nM
-
potato carboxypeptidase inhibitor
-
-
-
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
-
tick carboxypeptidase inhibitor
-
TCI
-
tick carboxypeptidase inhibitor
-
from Rhipicephalus bursa
-
Zn2+
-
effect of pH on Zn inhibition, ZnOH+ is inhibitory in vivo
Zn2+
at 0.1 mM 27.5% activity relative to control
additional information
-
substrate inhibition by: carbobenzoxy-Glyl-L-Phe, benzoyl-Gly-Phe
-
additional information
-
comparison of Ki-values of enzyme crystals and solution
-
additional information
-
enzyme acetylation reduces activity by 97%
-
additional information
-
study of pH-dependence of inhibition
-
additional information
-
study about coordination of low molecular weight inhibitors to metal ion
-
additional information
-
analysis of interactions between enzyme and multiple inhibitors using combination plots
-
additional information
-
mechanic strain may modify effect of inhibitors
-
additional information
-
molecular dynamics characterization of inhibitor adducts and structural variations induced by inhibitors
-
additional information
-
pH-dependent properties of Co enzymeûL-Phe complexes
-
additional information
-
no inhibition by erythro-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
additional information
-
no inhibition by (2R,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
additional information
-
no inhibition by N-(aminocarbonyl)phenylalanine up to 3.6 mM
-
additional information
-
synthesis of cyclen-containing inhibitors specific for CPA
-
additional information
-
rational design of mechanism-based irreversible enzyme inhibitors, inhibition mechanism, overview
-
additional information
-
no or poor inhibition by soybean Kunitz trypsin inhibitor, E64, leupeptin, chymostatin, pepstatin A, N-tosyl-L-lysine chloromethyl ketone, N-tosyl-L-phenylalanine chloromethyl ketone, iodoacetic acid
-
additional information
-
no inhibition by pyrantel tartrate, 12.5% in the anthelmintic drug Banminth
-
additional information
-
sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A, synthesis, overview
-
additional information
-
O-glycosidase has no effect in monocyte-derived macrophages. CPVL in THP-1 and Jurkat cell lines are insensitive to treatment with a cocktail of O-glycosidase, N-glycosidase and endoglycosidase H
-
additional information
-
dramatic excess substrate inhibition
-
additional information
-
feeding of the laravae on broccoli foliage reduces the enzyme activity in the midgut
-
additional information
PMSF at 2 mM, E-64 at 0.001 mM and Mn2+, Ni2+, Ca2+ and Mg2+ at 1 mM have no effect on activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.313
(S)-hippuryl-alpha-MePhe
-
pH 7.5
0.344
(S)-hippuryl-alpha-methylphenyllactic acid
-
pH 7.5
0.072
(S)-hippuryl-OPhe
-
pH 7.5
0.372
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0233
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0194
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.04
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0556
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0615
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0573
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0016
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-L-beta-phenyllactate
-
-
0.0135
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe
-
-
0.227 - 0.78
angiotensin I
0.1
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
1
benzoyl-Gly-Gly-L-Phe
-
-
0.2
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
0.23 - 11
benzoyl-Gly-L-Phe
0.051 - 0.088
benzoyl-Gly-phenyllactate
-
-
0.14
Benzyloxycarbonyl-Ala-Phe
-
-
0.31
Benzyloxycarbonyl-Gly-Phe
-
-
0.23
Benzyloxycarbonyl-Phe-Leu
-
-
0.74
Carbobenzoxy-Gly-Gly-Leu
-
-
1.34
Carbobenzoxy-Gly-Gly-Phe
-
-
2.11
carbobenzoxy-Gly-Gly-Val
-
-
0.16 - 33
carbobenzoxy-Gly-L-Leu
0.21 - 37
carbobenzoxy-Gly-L-Phe
6.1 - 14.3
carbobenzoxy-Gly-L-Trp
0.15 - 0.19
cinnamoyl-L-phenyllactate
-
-
0.02
hippuryl-DL-beta-phenylacetic acid
-
-
780 - 1300
hippuryl-DL-beta-phenyllactate
0.15
hippuryl-DL-phenyllactate
-
-
0.075
hippuryl-L-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
0.062 - 0.11
hippuryl-L-phenyllactate
0.7
hippuryl-Phe
-
pH 7.5
0.000124
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester
-
-
0.0124
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester
-
-
0.000223
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester
-
-
0.165
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.55
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.00923
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.065
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25°C, recombinant enzyme
0.0043
methotrexate-alpha-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
0.1
N-(2-furanacryloyl)-Phe-Phe
-
-
0.024 - 0.034
N-(3-[2-furyl]acryloyl)-Phe-Phe
0.44
N-acetyl-Gly-L-phenyllactic acid
-
-
0.74 - 6.53
N-carbobenzoxy-Gly-Gly-L-Leu
0.0346 - 0.314
N-carbobenzoxy-Gly-Gly-L-Phe
0.0449 - 0.985
N-carbobenzoxy-Gly-L-Phe
0.143 - 0.145
N-carbobenzoxy-Gly-L-Tyr
0.05
N-trans-3-(-3-indoleacryloyl)-L-Phe
-
-
27 - 340
N-[3-(2-furyl)acryloyl]-Phe-Phe
0.000329
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.49 - 120
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
additional information
additional information
-
0.227
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.23
benzoyl-Gly-L-Phe
-
at 0.1-0.4 mM substrate
0.45
benzoyl-Gly-L-Phe
-
-
0.8 - 11
benzoyl-Gly-L-Phe
-
-
10
benzoyl-Gly-L-Phe
-
at 1-10 mM substrate
0.16
carbobenzoxy-Gly-L-Leu
-
-
33
carbobenzoxy-Gly-L-Leu
-
mixture of isoenzyme 2 and 3
0.21
carbobenzoxy-Gly-L-Phe
-
-
0.71
carbobenzoxy-Gly-L-Phe
-
-
1.95 - 37
carbobenzoxy-Gly-L-Phe
-
-
2 - 37
carbobenzoxy-Gly-L-Phe
-
-
3
carbobenzoxy-Gly-L-Phe
-
at 1-4 mM substrate
13.3
carbobenzoxy-Gly-L-Phe
-
at 4-40 mM substrate
16.1
carbobenzoxy-Gly-L-Phe
-
mixture of isoenzyme 2 and 3
6.1 - 7.2
carbobenzoxy-Gly-L-Trp
-
-
14.3
carbobenzoxy-Gly-L-Trp
-
mixture of isoenzyme 2 and 3
780
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248F
1300
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25°C, wild-type enzyme
0.33
hippuryl-L-Phe
-
-
0.81 - 11
hippuryl-L-Phe
-
-
1.07
hippuryl-L-Phe
-
soluble enzyme
1.65
hippuryl-L-Phe
-
immobilized enzyme
3.3
hippuryl-L-Phe
-
pH 7.5, 25°C, mutant enzyme Y248A
5.6
hippuryl-L-Phe
-
pH 7.5, 25°C, mutant enzyme Y248F
60
hippuryl-L-Phe
-
pH 7.5, 25°C, wild-type enzyme
0.062
hippuryl-L-phenyllactate
-
-
0.11
hippuryl-L-phenyllactate
-
-
0.11
hippuryl-L-phenyllactate
-
mixture of isoenzyme 2 and 3
0.024
N-(3-[2-furyl]acryloyl)-Phe-Phe
in the absence of Co2+
0.034
N-(3-[2-furyl]acryloyl)-Phe-Phe
in the presence of Co2+
0.74
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 1
6.53
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 2
0.0346
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 1
0.314
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 2
0.0449
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 1
0.985
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 2
0.143
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 1
0.145
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 2
27
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, mutant enzyme Y248A
76
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, mutant enzyme Y248F
340
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, wild-type enzyme
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
0.5
ochratoxin A
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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
-
Km values of immobilized enzyme generally higher than those in solution
-
additional information
additional information
-
approximations for several substrates: 0.01 mM
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.33
(S)-hippuryl-alpha-MePhe
-
pH 7.5
477
(S)-hippuryl-alpha-methylphenyllactic acid
-
pH 7.5
682
(S)-hippuryl-OPhe
-
pH 7.5
24.3
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
12.4
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
13.4
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
23.9
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
44.3
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
57.3
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
19.4
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.062
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-L-beta-phenyllactate
-
-
1.18
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe
-
-
8.23
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
767
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
13.3 - 20
benzoyl-Gly-Gly-L-Phe
505
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
11.7 - 183
benzoyl-Gly-L-Phe
467 - 583
benzoyl-Gly-phenyllactate
-
-
89
Benzyloxycarbonyl-Ala-Phe
-
-
4.2
Benzyloxycarbonyl-Gly-Phe
-
-
66
Benzyloxycarbonyl-Phe-Leu
-
-
85
carbobenzoxy-Gly-Gly-L-Tyr
-
-
5.02
Carbobenzoxy-Gly-Gly-Leu
-
-
11.9
Carbobenzoxy-Gly-Gly-Phe
-
-
6.13
carbobenzoxy-Gly-Gly-Val
-
-
29
carbobenzoxy-Gly-L-Leu
-
mixture of isoenzyme 2 and 3
14.7 - 200
carbobenzoxy-Gly-L-Phe
29.8 - 90.5
carbobenzoxy-Gly-L-Trp
1.28
Carbobenzoxy-Gly-Leu
-
-
5.85
Carbobenzoxy-Gly-Phe
-
-
76.7
cinnamoyl-L-phenyllactate
-
-
0.1 - 0.39
hippuryl-DL-beta-phenyllactate
0.081
hippuryl-DL-phenyllactate
-
-
635
hippuryl-DL-phenyllactic acid
-
-
4.3
hippuryl-L-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
454 - 1000
hippuryl-L-phenyllactate
0.276
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester
-
-
0.725
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester
-
-
0.46
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester
-
-
2.33
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
3.43
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
1.45
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.09
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25°C, recombinant enzyme
1.9
methotrexate-alpha-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
667
N-(2-furanacryloyl)-Phe-Phe
-
-
7.6 - 11
N-(3-[2-furyl]acryloyl)-Phe-Phe
86
N-acetyl-Gly-L-phenyllactic acid
-
-
14 - 199
N-carbobenzoxy-Gly-Gly-L-Leu
57 - 97
N-carbobenzoxy-Gly-Gly-L-Phe
16.8 - 22.4
N-carbobenzoxy-Gly-L-Phe
14.4 - 26.2
N-carbobenzoxy-Gly-L-Tyr
0.05 - 1
N-[3-(2-furyl)acryloyl]-Phe-Phe
0.24
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.11 - 6.08
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
0.042
p-nitrophenyl acetate
-
-
additional information
additional information
-
13.3
benzoyl-Gly-Gly-L-Phe
-
-
20
benzoyl-Gly-Gly-L-Phe
-
-
11.7
benzoyl-Gly-L-Phe
-
at 0.1-0.4 mM substrate
66.7
benzoyl-Gly-L-Phe
-
at 1-10 mM substrate
93.3 - 183
benzoyl-Gly-L-Phe
-
-
14.7
carbobenzoxy-Gly-L-Phe
-
-
48.3
carbobenzoxy-Gly-L-Phe
-
at 1-4 mM substrate
90 - 198
carbobenzoxy-Gly-L-Phe
-
-
91.7 - 200
carbobenzoxy-Gly-L-Phe
-
-
112
carbobenzoxy-Gly-L-Phe
-
at 4-40 mM substrate
139
carbobenzoxy-Gly-L-Phe
-
mixture of isoenzyme 2 and 3
29.8
carbobenzoxy-Gly-L-Trp
-
mixture of isoenzyme 2 and 3
73.4 - 90.5
carbobenzoxy-Gly-L-Trp
-
-
0.1
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25°C, wild-type enzyme
0.39
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25°C, mutant enzyme Y248F
0.88
hippuryl-L-Phe
-
pH 7.5, 25°C, wild-type enzyme
4
hippuryl-L-Phe
-
pH 7.5, 25°C, mutant enzyme Y248F
5.1
hippuryl-L-Phe
-
pH 7.5, 25°C, mutant enzyme Y248A
6.08
hippuryl-L-Phe
-
pH 7.5, 25°C, wild-type enzyme
454
hippuryl-L-phenyllactate
-
-
933
hippuryl-L-phenyllactate
-
-
1000
hippuryl-L-phenyllactate
-
mixture of isoenzyme 2 and 3
5.98
hippuryl-Phe
-
-
7.6
N-(3-[2-furyl]acryloyl)-Phe-Phe
in the absence of Co2+
11
N-(3-[2-furyl]acryloyl)-Phe-Phe
in the presence of Co2+
14
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 2
199
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 1
57
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 1
97
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 2
16.8
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 2
22.4
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 1
14.4
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 1
26.2
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 2
0.05
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, wild-type enzyme
0.55
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, mutant enzyme Y248F
1
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25°C, mutant enzyme Y248A
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
additional information
additional information
-
-
-
additional information
additional information
-
comparison of turnover numbers of enzyme crystals and solution
-
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0.0011
(+-)-2-benzylsuccinic acid
-
-
0.00001
(2E)-2-mercapto-3-phenylacrylic acid
-
pH 7.5, 25°C
0.0021
(2E)-2-mercapto-4-phenylbut-2-enoic acid
-
pH 7.5, 25°C
0.00135
(2E)-2-mercapto-5-phenylpent-2-enoic acid
-
pH 7.5, 25°C
5.4 - 5.7
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
0.3 - 1.1
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
2.79
(2R,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
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
1.1 - 2.2
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
0.19
(2S,3R)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
3.86
(2S,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
pH 7.5
0.56
(2S,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
pH 7.5
1.46
(R)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
1.4
(R)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
pH 7.5
0.00015
(R)-2-benzyl-3-nitropropanoic acid
-
-
0.00043
(R)-2-benzyl-5-nitro-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.405
(R)-hippuryl-alpha-MePhe
-
pH 7.5
0.00036
(R)-N-(2-chloroethyl)-N-methylphenylalanine
-
pH 7.5
0.072
(R)-N-(N-hydroxysulfamoyl)phenylalanine
0.033
(R)-N-benzylcysteine
-
pH 7.5, 25°C
0.0079
(R)-N-cyclohexylcysteine
-
pH 7.5, 25°C
0.00056
(R)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
0.039
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
0.0029
(R)-N-isopropylcysteine
-
pH 7.5, 25°C
0.00061
(R)-N-phenethylcysteine
-
pH 7.5, 25°C
0.47
(R)-N-sulfamoylphenylalanine
0.00209
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
pH 7.5
0.1
(RS)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
0.00079
(RS)-2-benzyl-3-nitropropanoic acid
-
-
0.00353
(RS)-2-benzyl-3-sulfamoylpropionic acid
-
pH 7.5
0.002
(RS)-2-isobutyl-3-nitropropanoic acid
-
-
0.00038
(RS)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
pH 7.5
0.00011
(RS)-2-mercaptomethyl-2-methylbutanoic acid
-
pH 7.5
0.0001
(RS)-2-mercaptomethylbutyric acid
-
pH 7.5
0.00198
(RS)-3-phenyl-2-sulfamoyloxypropionic acid
-
pH 7.5
0.00209
(RS)-N-(hydroxyaminocarbonyl)-phenylalanine
-
pH 7.5
0.067
(RS)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
0.00142
(RS)-N-sulfamoylphenylalanine
-
pH 7.5
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
0.74
(S)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
2.9
(S)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
pH 7.5
0.068
(S)-2-benzyl-3-nitropropanoic acid
-
-
0.00016
(S)-2-benzyl-5-nitro-4-oxopentanoic acid
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0025
(S)-N-(2-chloroethyl)-N-methylphenylalanine
-
pH 7.5
0.035
(S)-N-(N-benzylsulfamoyl)phenylalanine
pH 7.5
0.0032
(S)-N-(N-hydroxysulfamoyl)phenylalanine
0.61
(S)-N-(N-isopropylsulfamoyl)phenylalanine
pH 7.5
0.18
(S)-N-(N-methylsulfamoiyl)phenylalanine
pH 7.5
0.18
(S)-N-(N-phenylethylsulfamoyl)phenylalanine
pH 7.5
0.00019
(S)-N-benzylcysteine
-
pH 7.5, 25°C
0.0029
(S)-N-cyclohexylcysteine
-
pH 7.5, 25°C
0.00495
(S)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
1.9
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
0.00056
(S)-N-isopropylcysteine
-
pH 7.5, 25°C
3.5
(S)-N-methyl-N-sulfamoylphenylalanine
pH 7.5
0.000055
(S)-N-phenethylcysteine
-
pH 7.5, 25°C
0.00065
(S)-N-sulfamoylphenylalanine
-
pH 7.5
0.00065
(S)-N-sulfamoylphenylalanine benzyl ester
pH 7.5
0.00529
2-(1-hydroxy-5-oxopyrrolidin-2-yl)-3-phenylpropanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.000011
2-benzyl-3-mecaptopropionate
-
-
0.00015
2-benzyl-3-nitropropanoic acid
-
-
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
0.207
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
0.0242
3-hydroxyaminocarbonyl-2-benzylpropanoic acid
-
pH 7.5, 25°C
0.062 - 6.1
3-Phenylpropionic acid
0.00806
3-[acetyl(hydroxy)amino]-2-benzylpropanoic acid
-
25°C, limiting value for Ki-value at intermediate pH
0.118
4-phenylbutyric acid
-
-
0.039
aminobenzylsuccinic acid
-
-
0.0055
anilino(mercapto)acetic acid
-
-
0.0000239
Ascaris carboxypeptidase inhibitor
-
-
-
0.00000071
CBZ-Ala-Gly-PSI[P(O2)O]-Phe
-
crystallographic study of structure
0.00154
D-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25°C
0.0015
D-N-hydroxyaminocarbonyl phenylalanine
-
1.2
D-penicillamine
-
zinc carboxypeptidase A
0.078
indole acetic acid
-
-
0.01898
L-N-(aminocarbonyl)phenylalanine
-
pH 7.5, 25°C
0.00456
L-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25°C
0.0046
L-N-hydroxyaminocarbonyl phenylalanine
-
1.7
L-Penicillamine
-
zinc carboxypeptidase A
0.0021
L-Phe-phosphoramidate-phenylester
-
-
0.058
L-Phenyllactate
-
-
0.0000073
leech carboxypeptidase inhibitor
-
-
-
0.0024
mercapto(methylamino)acetic acid
-
pH 7.5, 25°C
0.00022
mercaptoacetyl-D-Phe
-
-
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
0.0021
N-phenylphosphoryl-L-phenylalanine
-
-
2.5
p-nitrophenylacetic acid
-
-
0.001
Phe phosphonate
-
-
0.39
phenylacetic acid
-
-
0.000001
polypeptide inhibitor
-
molecular weight 10000
-
0.0000013 - 0.000107
potato carboxypeptidase inhibitor
-
0.0000069
potato carboxypeptidase inhibitor mutant DELTA39
-
-
-
0.0000185
potato carboxypeptidase inhibitor mutant F23A
-
pH 7.5
-
0.00044
potato carboxypeptidase inhibitor mutant F23A/W28A
-
pH 7.5
-
0.0000023
potato carboxypeptidase inhibitor mutant H15A
-
pH 7.5
-
0.0000015
potato carboxypeptidase inhibitor mutant N29A
-
pH 7.5
-
0.0000019
potato carboxypeptidase inhibitor mutant N29A/S30A
-
pH 7.5
-
0.0000035
potato carboxypeptidase inhibitor mutant N29G
-
pH 7.5
-
0.000125
potato carboxypeptidase inhibitor mutant P36G
-
-
-
0.0000014
potato carboxypeptidase inhibitor mutant S30A
-
pH 7.5
-
0.0000079
potato carboxypeptidase inhibitor mutant W22A
-
pH 7.5
-
0.0000132
potato carboxypeptidase inhibitor mutant W28A
-
pH 7.5
-
0.0000056
potato carboxypeptidase inhibitor mutant Y37G
-
-
-
0.000347
potato carboxypeptidase inhibitor mutant Y37G/DELTA39
-
-
-
0.00235
rac-2-(mercaptomethyl)-3-cyclohexylpropanoic acid
-
pH 7.5, 25°C
0.00016
rac-2-(mercaptomethyl)-4-methylpentanoic acid
-
pH 7.5, 25°C
0.000011
rac-2-benzyl-3-mercaptopropanoic acid
-
pH 7.5, pH 25°C
0.0016
rac-2-benzyl-5-chloropentanoic acid
-
pH 7.5
0.00081
rac-N-(1-naphthylmethyl)cysteine
-
pH 7.5, 25°C
0.0585
rac-N-(aminocarbonyl)phenylalanine
-
pH 7.5, 25°C
0.0094
rac-N-(cyclohexylmethyl)cysteine
-
pH 7.5, 25°C
0.00209
rac-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25°C
0.00085
rac-N-(p-methoxy)benzylcysteine
-
pH 7.5, 25°C
0.012
rac-N-benzyl-N-methylcysteine
-
pH 7.5, 25°C
0.00027
rac-N-benzylcysteine
-
pH 7.5, 25°C
0.0096
rac-N-cyclohexylcysteine
-
pH 7.5, 25°C
0.0014
rac-N-ethylcysteine
-
pH 7.5, 25°C
0.0075
rac-N-isobutylcysteine
-
pH 7.5, 25°C
0.0011
rac-N-isopropylcysteine
-
pH 7.5, 25°C
0.000065
rac-N-phenethylcysteine
-
pH 7.5, 25°C
0.0013
rac-N-phenylpropylcysteine
-
pH 7.5, 25°C
0.0056
rac-N-propylcysteine
-
pH 7.5, 25°C
0.0013
rac2-(mercaptomethyl)-6-phenylhexanoic acid
-
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
0.0000008
tick carboxypeptidase inhibitor
-
-
-
0.0000016
wild-type potato carboxypeptidase inhibitor
-
pH 7.5
-
additional information
additional information
-
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
0.3
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, mutant enzyme Y248F
0.34
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, substrate: hippuryl-L-Phe
0.35
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, wild-type enzyme
1.1
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25°C, mutant enzyme Y248A
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
0.072
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.072
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.039
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.039
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.47
(R)-N-sulfamoylphenylalanine
-
pH 7.5
0.47
(R)-N-sulfamoylphenylalanine
pH 7.5
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
0.0032
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.0032
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
1.9
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
1.9
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.062
3-Phenylpropionic acid
-
-
0.482
3-Phenylpropionic acid
-
-
6.1
3-Phenylpropionic acid
-
-
0.0023
D-Cys
-
pH 7.5, 25°C
0.0023
D-Cys
-
zinc carboxypeptidase A
0.074
D-Phe
-
-
0.35
L-Cys
-
pH 7.5, 25°C
0.35
L-Cys
-
zinc carboxypeptidase A
0.000003
latexin
-
-
-
0.000003
latexin
-
pH 7.5, recombinant CPA4
-
0.0000013
potato carboxypeptidase inhibitor
-
-
-
0.0000017
potato carboxypeptidase inhibitor
-
-
-
0.000002
potato carboxypeptidase inhibitor
-
-
-
0.000005
potato carboxypeptidase inhibitor
-
-
-
0.000107
potato carboxypeptidase inhibitor
-
-
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
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
-
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105700
-
biotin-PEG(5000)-carboxypeptidase complex, stoichiometry with avidin 1 : 1, determined by MALDI-TOF
130000
-
Western blot analysis
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
30000
-
boundary depletion sedimentation equilibrium
33520
predicted molecular mass, clone ID AM2-51, carboxypeptidase A
34370
-
amino acid analysis
34400
-
SDS-PAGE, type beta
34490
-
amino acid sequence
34600
-
SDS-PAGE, type gamma
34650
predicted molecular mass, clone ID AM1-02, carboxypeptidase A
34800
-
sedimentation equilibrium
34860
predicted molecular mass, clone ID AM1-72, carboxypeptidase A homolog
34870
predicted molecular mass, clone ID AM2-60, carboxypeptidase A
34900
predicted molecular mass, clone ID AM1-30, carboxypeptidase A homolog
35470
-
alpha form, amino acid analysis
35780
-
mature enzyme after cleavage of the signal- and activation peptides
37000
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
37800
-
SDS-PAGE, component II
38000
-
native ASPA expessed in COS-7 cells, determined by immunoblotting
39300
-
SDS-PAGE, component I
47140
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
47570
theoretical molecular mass MDCP-A2
47790
theoretical molecular mass MDCP-A1d
47820
theoretical molecular mass MDCP-A1a
47850
theoretical molecular mass MDCP-A1e
48500
-
calculated from cDNA
48730
-
calculated from amino acid sequence
52000
-
recombinant human ASPA fused to N-terminal thioredoxin and C-terimal V5 and a 6x-histidine tag, analyzed by SDS-PAGE
53600
-
calculated from amino acid sequence
58000
x * 58300, sequence analysis, x * 58000, polyclonal anti-MCP-2 peptide serum
58300
x * 58300, sequence analysis, x * 58000, polyclonal anti-MCP-2 peptide serum
80000
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
34000
-
gel filtration
34000
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
34990
predicted molecular mass, clone ID AM3-75, carboxypeptidase A
34990
predicted molecular mass, clone ID L4-60, carboxypeptidase A
35000
-
gel filtration
35000
-
sedimentation equilibrium
35000
-
in presence of urea and 2-mercaptoethanol, SDS-PAGE
36000
-
fully processed form of MC-CPA, SDS-PAGE
36000
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
40000
-
gel filtration
40000
-
1 * 40000, SDS-PAGE
42000
-
determined by SDS-PAGE and Western blotting
42000
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
47890
theoretical molecular mass MDCP-A1b
47890
theoretical molecular mass MDCP-A1c
additional information
-
molecular weight of dimeric procarboxypeptidase 72500
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
additional information
enzyme-inhibitor complex
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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
A305E
-
tested Canavan Disease mutation, results in undetectable enzyme activity
A57T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
C124A
-
alanine substitution of Cys124, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152A
-
alanine substitution of Cys152, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152W
-
tested Canavan Disease mutation, results in undetectable enzyme activity
C61A
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61S
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61W
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D204H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D249V
-
tested Canavan Disease mutation, results in undetectable enzyme activity
D68A
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E178A
-
mutation of the general proton donor
E214X
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E24D
-
mutation of a putative zinc-binding residue
E24G
-
mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity
E24H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
E24H/H116E
-
mutant designed to switch the order of the zinc-binding residues
E285A
-
tested Canavan Disease mutation
F295S
-
untested Canavan Disease mutation, results in undetectable enzyme activity
G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
H116E
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
H116G
-
mutation of a putative zinc-binding residue
H21E/E24H
-
mutant designed to switch the order of the zinc-binding residues
H21G
-
mutation of a putative zinc-binding residue
H21P
-
untested Canavan Disease mutation, results in undetectable enzyme activity
I143T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
K213E/G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
M195R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
P183H
-
untested Canavan Disease mutation
R127A
-
the mutation causes kcat to decrease from 12 to 0.012 which corresponds to a 6 kcal/mol decrease in the stabilization of transition state in the rate determining step
R63N
-
mutation that affects transition state stabilization
R71N
-
mutation that affects substrate carboxyl binding
E378A
-
Glu378 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L
-
Tyr356 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L/E378A
-
mutant expresses about 80% of the amount of Mc-cpa compared to the wild type enzyme, the mutant enzyme lacks activity
additional information
-
mice lacking Nna1/CCP1 show absence of the detyrosinylated form of alpha-tubulin in mitral cells
additional information
-
in agiotensin-converting enzyme -/- mice the addition of the carboxypeptidase A inhibitor benzylsuccinate essentially abolishs the formation of Ang(1-9) and increases the levels of angiotensin I in cardiac membranes
additional information
-
mice lacking Nna1/CCP1 show absence of the detyrosinylated form of alpha-tubulin in mitral cells
-
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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
additional information
-
PTD012 might not belong to the carboxypeptidase family of enzymes, might belong to the superfamily of metallo-beta-lactamase fold proteins
analysis
the enzyme can serve as specific molecular maker for mast cells amongst normal hematopoietic cell populations
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
biotechnology
-
a strategy is shown for the expression of MeCPA-His6PR in the cytosol of Escherichia coli and a relatively simple procedure to purify it to homogeneity. The bacterial system yields about 0.5 mg of pure enzyme per liter of cell culture and is more convenient and less expensive than is the production of MeCPA in insect cells
drug development
the enzyme is a target for drug development for biotechnological and biomedical applications
drug development
-
the enzyme serves as model enzyme for design of specific inhibiors for zinc proteases
drug development
potential target for drug development
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
food industry
-
the application of the novel ochratoxin A hydrolytic enzyme to reduce the ochratoxin A contents on some food or feed products is under evaluation
food industry
-
application of enzyme to wheat flour contaminated by ochratoxin A leads to 16.8-78.5% reduction of ochratoxin A and production of ochratoxin alpha
food industry
-
application of enzyme to wheat flour contaminated by ochratoxin A leads to 16.8-78.5% reduction of ochratoxin A and production of ochratoxin alpha
medicine
-
design of mechanism-based, specific inhibitors to cure disease caused by enzyme overfunction
medicine
-
evaluation of an antibody-directed enzyme-prodrug therapy for anticancer treatment using the A33 antigen, the enzyme, and methotrexate-phenylalanine as prodrug, overview
medicine
-
assay of total-carboxypeptidase A, the active form of CPA and pro CPA, in serum might be useful for the surveillance of early-stage pancreatic carcinoma
medicine
-
carboxypeptidase A is an interesting biomedical target enzyme as it is involved in prostate cancer
medicine
-
fusion protein design is successful in providing targeted inhibition of tumor growth in prostate cancer, the design can be used to construct other fusion genes
medicine
-
increased activity of carboxypeptidase A has been demonstrated in plasma samples from patients with pancreatitis
medicine
-
mast cell-proteases are considered as promising drug targets
medicine
-
mc-CPA is an essential effector molecule providing a very rapid and life-saving response of toxin neutralization in vivo
medicine
-
mutations that results in near undetectable activity of aspartocyclase correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood
medicine
results offer new opportunities for intervention and therapy of initiation and progression of autoimmune diseases
medicine
-
the avidin-biotin-PEGylated-carboxypeptidase complex has a great potential as a therapeutic protein delivery system for solid tumor prodrug targeting
medicine
engaged in prostate cancer
medicine
addition of CPA-directed antibodies to Plasmodium berghei-containing blood meal significantly reduces the mosquito infection rate in the test group compared to control and blocks the parasite development in the midgut
medicine
-
knock-down of CPA4 decreases cancer cell proliferation of Bel-7402 cells. In serum-free culture, downregulated CPA4 suppresses the sphere formation capacities of tumour cells. Upregulated CPA4 in Hep-G2 cells increases the proliferation and sphere formation capacity. The protein expression of CD133, ALDH1 and CD44 also increases in cells with upregulated CPA4. In vivo, the overexpression of CPA4 in tumour cells that are subcutaneously injected into nude mice markedly increases the growth of the tumours
synthesis
-
enzymatic modification of human haemoglobin, useful for functional studies
synthesis
-
immobilization for synthetic use
synthesis
-
useful tools for peptide biosynthesis in non-conventional media, considered
synthesis
-
procedure for the production of CPA in the cytosol of Escherichia coli that yields approximately 0.5 mg of pure enzyme per liter of cell culture. The expression strategy maintains the proCPA zymogen in a soluble state by fusing it to the C-terminus of maltose-binding protein while simultaneously overproducing the protein disulfide isomerase DsbC in the cytosol from a separate plasmid. The yield of active and properly oxidized CPA is highest when coexpressed with DsbC in BL21(DE3) cells that do not also contain mutations in the trxB and gor genes. Most of the active CPA is generated after cell lysis and amylose affinity purification of the MBP-proCPA fusion protein, during the time that the partially purified protein is held overnight at 4°C prior to activation with thermolysin