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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-beta-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 inhibtion
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
-
-
-