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4-acetyloxyproline-2-naphthylamide + H2O
2-naphthylamine + 4-acetyloxyproline
-
-
-
?
Ala-4-nitroanilide + H2O
L-alanine + p-nitroaniline
Ala-beta-naphthylamide + H2O
Ala + beta-naphthylamine
-
-
-
?
Ala-Pro + H2O
L-alanine + L-proline
-
-
-
?
Arg-Pro-Pro + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Gly-p-nitroanilide + H2O
glycine + p-nitroaniline
Gly-Pro-4-nitroanilide + H2O
?
-
-
-
?
glycyl-2-naphthylamide + H2O
glycine + 2-naphthylamine
-
6.4% of the activity with L-prolyl-2-naphthylamide
-
-
?
His-p-nitroanilide + H2O
L-histidine + p-nitroaniline
Hyp-2-naphthylamide + H2O
Hyp + 2-naphthylamine
Hyp-beta-naphthylamide + H2O
Hyp + beta-naphthylamine
-
-
-
?
Hyp-Gly + H2O
Hyp + Gly
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
L-alanyl-2-naphthylamide + H2O
L-alanine + 2-naphthylamine
-
6.1% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-arginyl-2-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
3.2% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-histidinyl-2-naphthylamide + H2O
L-histidine + 2-naphthylamine
-
6.3% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
2-naphthylamine + L-hydroxyproline
-
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
L-hydroxyprolyl-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
L-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
-
4.7% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys 4-nitroaniline
-
-
-
-
?
L-phenylalanyl-2-naphthylamide + H2O
L-phenylalanine + 2-naphthylamine
-
7.6% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
L-Pro-L-Ala + H2O
L-Pro + L-Ala
-
no activity of mutant R136A
-
?
L-Pro-L-Leu-Gly-NH2 + H2O
L-Pro + L-Leu-Gly-NH2
-
-
-
-
?
L-Pro-L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
L-proline beta-naphthylamide + H2O
L-proline + 2-naphthylamine
-
-
-
?
L-proline-4-nitroanilide + H2O
L-proline + 4-nitroaniline
L-proline-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
enzyme displays a 50fold specificity for cleaving N-terminal Pro-X compared with Ala-X or Val-X bonds
-
-
?
L-prolyl-2-naphthylamide + H2O
L-proline + 2-naphthylamine
-
-
-
-
?
L-prolyl-4-nitroanilide + H2O
L-proline + 4-nitroaniline
L-prolyl-p-nitroanilide + H2O
L-proline + p-nitroaniline
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
Leu-Pro-Pro-Ser-Arg + H2O
?
-
-
-
-
?
Lys-4-nitroanilide + H2O
L-lysine + p-nitroaniline
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
PLSRTLSVAAKK + H2O
LSRTLSVAAKK + L-proline
-
-
-
?
PLSRTLSVAAKK + H2O
Pro + LSRTLSVAAKK
-
-
-
?
poly-(L-Pro) + H2O
proline
-
no hydrolysis
-
-
?
PPGFSPFR + H2O
PGFSPFR + L-proline
-
-
-
?
PPGFSPFR + H2O
Pro + PGFSPFR
-
-
-
?
Pro-2-naphthylamide + H2O
2-naphthylamine + L-proline
-
-
-
?
Pro-2-naphthylamide + H2O
beta-naphthylamine + L-proline
-
-
-
?
Pro-2-naphthylamide + H2O
Pro + 2-naphthylamide
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Pro-4-nitroanilide + H2O
4-nitroaniline + L-proline
-
-
-
?
Pro-4-nitroanilide + H2O
L-proline + p-nitroaniline
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
Pro-7-amido-4-methylcoumarin + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
Pro-Ala + H2O
L-alanine + L-proline
-
-
-
?
Pro-Asp + H2O
Pro + Asp
-
-
-
-
?
Pro-beta-naphthylamide + H2O
Pro + beta-naphthylamine
Pro-D-Ala + H2O
Pro + D-Ala
-
-
-
-
?
Pro-D-Phe + H2O
Pro + D-Phe
-
-
-
-
?
Pro-Gly-Gly + H2O
Pro + Gly-Gly
low activity
-
-
?
Pro-Gly-Gly-Gly + H2O
Pro + Gly-Gly-Gly
low activity
-
-
?
Pro-Leu-Gly + H2O
Leu-Gly + Pro
-
-
-
?
Pro-Leu-Gly + H2O
Pro + Leu-Gly
low activity
-
-
?
Pro-Leu-Gly-NH2 + H2O
Leu-Gly-NH2 + L-proline
-
-
-
?
Pro-Leu-Gly-NH2 + H2O
Pro + Leu-Gly-NH2
-
-
-
-
?
Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys + H2O
Pro + Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys
17.4% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-p-nitroanilide + H2O
L-proline + p-nitroaniline
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
Pro-Phe-NH2 + H2O
Pro + Phe-NH2
-
-
-
-
?
Pro-Trp + H2O
Pro + Trp
-
-
-
-
?
proline beta-naphthylamide + H2O
proline + beta-naphthylamine
-
-
-
?
proline-7-amido-4-methylcoumarin + H2O
proline + 7-amino-4-methylcoumarin
-
-
-
?
Val-4-nitroanilide + H2O
L-valine + p-nitroaniline
additional information
?
-
Ala-4-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
Ala-4-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
Gly-p-nitroanilide + H2O
glycine + p-nitroaniline
-
-
-
-
?
Gly-p-nitroanilide + H2O
glycine + p-nitroaniline
-
-
-
-
?
His-p-nitroanilide + H2O
L-histidine + p-nitroaniline
-
-
-
-
?
His-p-nitroanilide + H2O
L-histidine + p-nitroaniline
-
-
-
-
?
Hyp-2-naphthylamide + H2O
Hyp + 2-naphthylamine
-
-
-
-
?
Hyp-2-naphthylamide + H2O
Hyp + 2-naphthylamine
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
-
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
oral microorganisms
-
enzymes II and III
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
no hydrolysis
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
-
-
-
?
L-hydroxyprolyl-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
-
-
?
L-hydroxyprolyl-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
-
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
Lyophyllum cinerascens
-
-
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
-
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
-
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
using ten different aminoacyl-pNA substrates. PAP only shows catalytic activity toward L-Pro-4-nitroanilide
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
highly selective
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
highly selective
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline-4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-proline-4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-prolyl-4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-prolyl-4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
no cleavage of NH2-group substituted proline
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
specific for N-terminal L-Pro residues
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
Lyophyllum cinerascens
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
hydrolytic activity decreases with increasing chain length
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
oral microorganisms
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
cleavage of D-Pro residues
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
-
-
-
?
Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
Lys-4-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
Lys-4-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
oral microorganisms
-
enzymes II and III specific for
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
-
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-nitroanilide + H2O
L-proline + p-nitroaniline
-
-
-
-
?
Pro-4-nitroanilide + H2O
L-proline + p-nitroaniline
-
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
-
-
?
Pro-Ala + H2O
Pro + Ala
PamA releases Pro from amino terminus of a dipeptide Pro-Ala, and not from Ala-Pro
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
-
?
Pro-Ala + H2O
Pro + Ala
low activity
-
-
?
Pro-beta-naphthylamide + H2O
Pro + beta-naphthylamine
docking into the catalytic site of PipA
-
-
?
Pro-beta-naphthylamide + H2O
Pro + beta-naphthylamine
preferred substrate
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
69.5% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Leu + H2O
Pro + Leu
69.5% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
-
?
Pro-Leu + H2O
Pro + Leu
low activity
-
-
?
Pro-Lys + H2O
Pro + Lys
-
-
-
?
Pro-Lys + H2O
Pro + Lys
74.4% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Lys + H2O
Pro + Lys
74.4% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Lys + H2O
Pro + Lys
-
-
-
?
Pro-Lys + H2O
Pro + Lys
-
-
-
-
?
Pro-p-nitroanilide + H2O
L-proline + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
L-proline + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
-
-
-
-
?
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
-
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
best peptide substrate
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
best peptide substrate
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
Pro-Pro + H2O
Pro + Pro
44.1% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Pro + H2O
Pro + Pro
44.1% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
Val-4-nitroanilide + H2O
L-valine + p-nitroaniline
-
-
-
-
?
Val-4-nitroanilide + H2O
L-valine + p-nitroaniline
-
-
-
-
?
additional information
?
-
hydrolysis of reice protein by wild-type and mutant enzymes
-
-
?
additional information
?
-
the enzyme cleaves N-terminal Pro residues from many peptides but shows varying hydrolysis rates for various Pro-X dipeptides or peptides of different lengths. The recombinant prolyl aminopeptidase hydrolyzes Pro-4-nitroanilide specifically and no activity is observed toward other 4-nitroanilide substrates. No activity with Leu-Pro. Enzyme PAP can act on casein
-
-
?
additional information
?
-
-
the enzyme cleaves N-terminal Pro residues from many peptides but shows varying hydrolysis rates for various Pro-X dipeptides or peptides of different lengths. The recombinant prolyl aminopeptidase hydrolyzes Pro-4-nitroanilide specifically and no activity is observed toward other 4-nitroanilide substrates. No activity with Leu-Pro. Enzyme PAP can act on casein
-
-
?
additional information
?
-
the enzyme cleaves N-terminal Pro residues from many peptides but shows varying hydrolysis rates for various Pro-X dipeptides or peptides of different lengths. The recombinant prolyl aminopeptidase hydrolyzes Pro-4-nitroanilide specifically and no activity is observed toward other 4-nitroanilide substrates. No activity with Leu-Pro. Enzyme PAP can act on casein
-
-
?
additional information
?
-
hydrolysis of reice protein by wild-type and mutant enzymes
-
-
?
additional information
?
-
-
not active with L-Phe-p-nitroanilide, L-Ala-p-nitroanilide, L-Leu-p-nitroanilide, casein, and benzyl-Arg-p-nitroanilide
-
-
?
additional information
?
-
-
substrate specificity, no activity with any other Xaa-7-amido-4-methylcoumarin substrate, no activity with substrates Leu-Pro, Leu-Leu, Val-Val, Gly-Pro, Lys-Lys, Glu-Glu, and Ala-Ala-Ala
-
?
additional information
?
-
-
enzyme possibly plays a role in meat fermentation
-
?
additional information
?
-
-
substrate specificity, no activity with any other Xaa-7-amido-4-methylcoumarin substrate, no activity with substrates Leu-Pro, Leu-Leu, Val-Val, Gly-Pro, Lys-Lys, Glu-Glu, and Ala-Ala-Ala
-
?
additional information
?
-
-
enzyme possibly plays a role in meat fermentation
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
-
the enzyme is a serine protease
-
-
?
additional information
?
-
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
the recombinant enzyme can cleave the peptides derived from enzyme-hydrolytic natural proteins to release free lysine
-
-
?
additional information
?
-
-
the recombinant enzyme can cleave the peptides derived from enzyme-hydrolytic natural proteins to release free lysine
-
-
?
additional information
?
-
enzyme releases L-lysine from various hydrolytic products of milk, BSA and collagen treated with the alkaline protease DHAP. No substrates: L-Leu-4-nitroanilide, L-Phe-4-nitroanilide, L-Tyr-4-nitroanilide Gly-Gly-Gly-4-nitroanilide, L-Ser-Gly-L-Arg-4-nitroanilide, L-Ala-L-Ala-L-Val4-nitroanilide, L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide, L-Ala-L-Ala-L-Val-L-Ala-4-nitroanilide
-
-
?
additional information
?
-
-
enzyme releases L-lysine from various hydrolytic products of milk, BSA and collagen treated with the alkaline protease DHAP. No substrates: L-Leu-4-nitroanilide, L-Phe-4-nitroanilide, L-Tyr-4-nitroanilide Gly-Gly-Gly-4-nitroanilide, L-Ser-Gly-L-Arg-4-nitroanilide, L-Ala-L-Ala-L-Val4-nitroanilide, L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide, L-Ala-L-Ala-L-Val-L-Ala-4-nitroanilide
-
-
?
additional information
?
-
the proline iminopeptidase, PchPiPA, catalyzes specific hydrolysis of N-terminal proline from peptides
-
-
?
additional information
?
-
-
the proline iminopeptidase, PchPiPA, catalyzes specific hydrolysis of N-terminal proline from peptides
-
-
?
additional information
?
-
PfPAPis a prolyl aminopeptidase with a preference for N-terminal proline substrates
-
-
?
additional information
?
-
-
PfPAPis a prolyl aminopeptidase with a preference for N-terminal proline substrates
-
-
?
additional information
?
-
the recombinant enzyme shows preference for substrates with a proline at the N-terminus. The enzyme also hydrolyzes beta-naphthylamides of hydroxyproline and alanine, although the observed activity is almost 2fold lower than against Pro-beta-naphthylamide. The activity against the other amino acid-beta-naphthylamides tested (with Phe-, Glu-, Arg-, Tyr-, Leu-, Asp-, Met-, Trp-, and Val-beta-naphthylamide) is not detectable or does not exceed 7% of the maximal activity. Among the peptides with proline at the N-terminus, TsPAP1 shows a much higher preference for dipeptides than tri- and tetrapeptides. Not only the length of the peptide is important, as also the amino acid in the Y position influences the rate of proline liberation. Among dipeptides, the most preferred is Pro-Gly and Pro-Pro while Pro-Ala is hydrolyzed at only 10% the rate of Pro-Gly. The activity against tripeptide Pro-Gly-Gly is 27% of the maximal activity while the rate of hydrolysis of the tetrapeptides is very low and does not exceed 10% of that against Pro-Gly
-
-
?
additional information
?
-
-
substrate specificity and binding mechanism
-
?
additional information
?
-
-
discussion of biological significance
-
-
?
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evolution
enzyme TsPAP1 belongs to the S33.001 subfamily of aminopeptidases
evolution
enzyme TsPAP1 belongs to the S33.001 subfamily of aminopeptidases with presence of additional tens of amino acids at the N-terminus of the most plant sequences but not of microorganisms. These additional amino acids constitute a potential signal peptide sequence most likely directing the proteins to chloroplasts. The plant PAP sequences display a high percent of amino acid identity from only the second methionine from the N-terminus (M86 in TsPAP1) while not within the sequence of the signal peptide
evolution
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
evolution
-
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
-
evolution
-
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
-
evolution
-
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
-
evolution
-
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
-
evolution
-
the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides
-
malfunction
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
malfunction
enzyme deletion lead to an increase in the deformability of parasite-infected red cells and in reduced adherence to the endothelial cell receptor CD36 under flow conditions
malfunction
impact of TsPAP1 overexpression on flowering time and the number of siliques due to the enhanced accumulation of proline in transgenic Arabidopsis thaliana plants, phenotype, overview
malfunction
-
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
-
malfunction
-
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
-
malfunction
-
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
-
malfunction
-
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
-
malfunction
-
disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain
-
metabolism
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
metabolism
-
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
-
metabolism
-
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
-
metabolism
-
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
-
metabolism
-
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
-
metabolism
-
PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth
-
physiological function
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
physiological function
prolyl aminopeptidases are specific exopeptidases, serine peptidases, that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. Specialized peptidases are essential to the degradation of proline-rich peptides and proteins, such as collagen and gelatin. Collagens, which contain an extremely high percentage of proline residues (20%), are composed of numerous repeats of a tripeptide, Gly-Pro-X
physiological function
TaPAP1 is involved in the plant response to zinc stress. Overexpressing of the Triticum aestivum prolyl aminopeptidase gene enhances zinc stress tolerance in transgenic Arabidopsis thaliana
physiological function
the Plasmodium falciparum S33 proline aminopeptidase is an exopeptidase associated with changes in erythrocyte deformability
physiological function
-
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
-
physiological function
-
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
-
physiological function
-
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
-
physiological function
-
prolyl aminopeptidases are specific exopeptidases, serine peptidases, that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. Specialized peptidases are essential to the degradation of proline-rich peptides and proteins, such as collagen and gelatin. Collagens, which contain an extremely high percentage of proline residues (20%), are composed of numerous repeats of a tripeptide, Gly-Pro-X
-
physiological function
-
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
-
physiological function
-
enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants
-
additional information
proline iminopeptidase, PchPiPA, molecular docking of substrate Pro-beta-naphthylamide, overview. The peptide bond in Pro-beta-naphthylamide is associated with Glu198, Ser107, and Gly40, respectively, via formation of hydrogen bond. Further, some hydrophobic residues, like Phe133, Phe143, Phe223, Val266, and Cys267, are surrounding the docked substrate to form the catalytic pocket with a channel protruding out of the molecular surface. The substrate is believed to diffuse into the catalytic pocket
additional information
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proline iminopeptidase, PchPiPA, molecular docking of substrate Pro-beta-naphthylamide, overview. The peptide bond in Pro-beta-naphthylamide is associated with Glu198, Ser107, and Gly40, respectively, via formation of hydrogen bond. Further, some hydrophobic residues, like Phe133, Phe143, Phe223, Val266, and Cys267, are surrounding the docked substrate to form the catalytic pocket with a channel protruding out of the molecular surface. The substrate is believed to diffuse into the catalytic pocket
additional information
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
additional information
the enzyme from Lactobacillus brevis shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
additional information
-
the enzyme from Lactobacillus corniformis shows about half of the activity of Lactobacillus plantarum strain NCDC 020 enzyme
additional information
the enzyme from Lactobacillus fermentum shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
additional information
the enzyme from Lactobacillus paracasei shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
additional information
the enzyme from Lactobacillus rhamnosus shows almost equally high activity compare to the enzyme from Lactobacillus plantarum strain NCDC 020
additional information
the enzyme from Pediococcus acidilactici shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
additional information
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
additional information
-
the enzyme from Lactobacillus brevis shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus paracasei shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus rhamnosus shows almost equally high activity compare to the enzyme from Lactobacillus plantarum strain NCDC 020
-
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
-
additional information
-
the enzyme from Lactobacillus brevis shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus paracasei shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
-
additional information
-
the enzyme from Lactobacillus rhamnosus shows almost equally high activity compare to the enzyme from Lactobacillus plantarum strain NCDC 020
-
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
-
additional information
-
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus corniformis shows about half of the activity of Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus brevis shows about one third of the activity of the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus fermentum shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
-
additional information
-
the enzyme from Lactobacillus fermentum shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
additional information
-
three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP
-
additional information
-
the enzyme from Lactobacillus acidophilus shows very low activity compared to the Lactobacillus plantarum strain NCDC 020 enzyme
-
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C267A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type, as well as reduced thermostability
D264H
mutation in educed catalytic residue, complete inactivation
E198A
site-directed mutagenesis, the mutation abolishes the enzyme activity
E198Q
site-directed mutagenesis, the mutation abolishes the enzyme activity
E227A
site-directed mutagenesis, the mutation abolishes the enzyme activity
F133A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type, as well as reduced thermostability
F143A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type, as well as reduced thermostability
F223A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type, as well as significantly reduced thermostability
F231A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type, as well as highly reduced thermostability
H292L
mutant shows no enzymatic activity
V266A
site-directed mutagenesis, almost inactive mutant
C271A
-
site-directed mutagenesis, sensitive to inhibition by 4-chloromercuribenzoic acid
C74A
-
site-directed mutagenesis, sensitive to inhibition by 4-chloromercuribenzoic acid
C74A/C271A
-
site-directed mutagenesis, not sensitive to inhibition by 4-chloromercuribenzoic acid
E204Q
-
site-directed mutagenesis, 4% of the wild-type catalytic efficiency
F139A
-
site-directed mutagenesis, 80fold decreased catalytic activity compared to the wild-type enzyme
R136A
-
site-directed mutagenesis, shows decreased activity compared to the wild-type enzyme, but retains arylamidase activity
Y149A
-
site-directed mutagenesis, unaltered catalytic efficiency compared to the wild-type enzyme
D246A
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
H273A
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
S106A
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
D246A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
H273A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
S106A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
D246A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
H273A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
S106A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
D246A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
H273A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
S106A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
D246A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
H273A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
S106A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
D246A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
H273A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
S106A
-
site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished
-
D264A
mutant shows no enzymatic activity
D264A
mutation in educed catalytic residue, complete inactivation
S107D
mutant shows no enzymatic activity
S107D
mutation in educed catalytic residue, complete inactivation
additional information
recombinant expression of enzyme Pap in Bacillus subtilis strain WB600. For cell culture, batch fermentation conditions, including the agitation speed, pH and temperature, are systematically optimized based on a kinetic analysis, fermentation kinetics, method optimization, overview. The yield of PAP reaches 174.8 U/ml under the optimized conditions, which is 1.66 times higher than that of the original production. The structure and storage stability of the lyophilized enzyme are significantly increased when protectants are added, and PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness
additional information
-
recombinant expression of enzyme Pap in Bacillus subtilis strain WB600. For cell culture, batch fermentation conditions, including the agitation speed, pH and temperature, are systematically optimized based on a kinetic analysis, fermentation kinetics, method optimization, overview. The yield of PAP reaches 174.8 U/ml under the optimized conditions, which is 1.66 times higher than that of the original production. The structure and storage stability of the lyophilized enzyme are significantly increased when protectants are added, and PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness
-
additional information
-
construction of chimera between the salt-sensitive enzyme from Streptomyces lividans and the salt-resistant enzyme from Streptomyces aureofaciens. The fine tuning of the N-terminal conformation of Streptomyces aureofaciens enzyme by hydrophobic interaction is important for the salt tolerance
additional information
-
construction of chimera between the salt-sensitive enzyme from Streptomyces lividans and the salt-resistant enzyme from Streptomyces aureofaciens. The fine tuning of the N-terminal conformation of Streptomyces aureofaciens enzyme by hydrophobic interaction is important for the salt tolerance
-
additional information
impact of TsPAP1 overexpression on flowering time and the number of siliques due to the enhanced accumulation of proline in transgenic Arabidopsis thaliana plants. The recombinant TsPAP1 protein is expressed without the signal peptide, which could have a negative impact on its activity
additional information
-
construction of chimera between the salt-sensitive enzyme from Streptomyces lividans and the salt-resistant enzyme from Streptomyces aureofaciens. The fine tuning of the N-terminal conformation of Streptomyces aureofaciens enzyme by hydrophobic interaction is important for the salt tolerance
additional information
overexpression of enzyme TaPAP1 from Triticum aestivum in transgenic Arabidopsis thaliana plants, zinc-stressed TaPAP1 transgenic Arabidopsis displays higher survival rate, fresh weight, photosynthetic efficiency, proline levels, and PAP activity compared to wild-type Arabidopsis thaliana plants
additional information
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disruption of gene results in significantly attenuated virulence of Xanthomonas campestris. Study on expression regulation
additional information
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
-
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
-
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
-
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
-
additional information
-
disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview
-
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-
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Purification and properties of a proline iminopeptidase from apricot seeds
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Substrate specifictiy of a proline iminopeptidase from apricot seeds
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Proline iminopeptidase. II. Purification and comparison with iminodipeptidase (prolidase)
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Purification and characterization of proline iminopeptidase from Lyophyllum cinerascens
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-
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Prolyl aminopeptidases from pig intestinal mucosa and human liver: Purification, characterization and possible identity with leucyl aminopeptidase
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-
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-
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The purification and characterization of prolyl aminopeptidase from Penicillium camemberti
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-
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Rattus norvegicus
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Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii
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Purification and characterization of a novel prolyl aminopeptidase from Maitake (Grifola frondosa)
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Neisseria gonorrhoeae
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Hynoenen, U.; Avall-Jaeaeskelaeinen, S.; Palva, A.
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Characterization of a unique proline iminopeptidase from white-rot basidiomycetes Phanerochaete chrysosporium
Biochimie
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Matsushita-Morita, M.; Furukawa, I.; Suzuki, S.; Yamagata, Y.; Koide, Y.; Ishida, H.; Takeuchi, M.; Kashiwagi, Y.; Kusumoto, K.I.
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Mahon, C.S.; ODonoghue, A.J.; Goetz, D.H.; Murray, P.G.; Craik, C.S.; Tuohy, M.G.
Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii
Microbiology
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Rasamsonia emersonii (Q8X1C7), Rasamsonia emersonii
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Ding, G.W.; Zhou, N.D.; Tian, Y.P.
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Szawlowska, U.; Grabowska, A.; Zdunek-Zastocka, E.; Bielawski, W.
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Navidghasemizad, S.; Takala, T.; Alatossava, T.; Saris, P.
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Nandan, A.S.; Nampoothiri, K.M.
Unveiling aminopeptidase P from Streptomyces lavendulae: molecular cloning, expression and biochemical characterization
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Li, N.; Wu, J.M.; Zhang, L.F.; Zhang, Y.Z.; Feng, H.
Characterization of a unique proline iminopeptidase from white-rot basidiomycetes Phanerochaete chrysosporium
Biochimie
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Phanerodontia chrysosporium (C6KI04), Phanerodontia chrysosporium
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Wang, K.D.; Wang, K.H.; Zhou, N.D.; Tian, Y.P.
Secretory expression, purification, characterization, and application of an Aspergillus oryzae prolyl aminopeptidase in Bacillus subtilis
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da Silva, F.L.; Dixon, M.W.; Stack, C.M.; Teuscher, F.; Taran, E.; Jones, M.K.; Lovas, E.; Tilley, L.; Brown, C.L.; Trenholme, K.R.; Dalton, J.P.; Gardiner, D.L.; Skinner-Adams, T.S.
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Kan, J.; An, L.; Wu, Y.; Long, J.; Song, L.; Fang, R.; Jia, Y.
A dual role for proline iminopeptidase in the regulation of bacterial motility and host immunity
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Wang, Y.; Liu, H.; Wang, S.; Li, H.; Xin, Q.
Overexpressing of a novel wheat prolyl aminopeptidase gene enhances zinc stress tolerance in transgenic Arabidopsis thaliana
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Triticum aestivum (A0A3B5Y450)
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Zdunek-Zastocka, E.; Grabowska, A.; Branicki, T.; Michniewska, B.
Biochemical characterization of the triticale TsPAP1, a new type of plant prolyl aminopeptidase, and its impact on proline content and flowering time in transgenic Arabidopsis plants
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Secale cereale x Triticum turgidum subsp. durum (G9J616)
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Wang, K.; Tian, Y.; Zhou, N.; Liu, D.; Zhang, D.
Studies on fermentation optimization, stability and application of prolyl aminopeptidase from Bacillus subtilis
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Aspergillus oryzae (W8GG09), Aspergillus oryzae JN-412 (W8GG09)
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Jing, Z.; Feng, H.
Studies on the molecular docking and amino acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis
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Yang, H.; Zhu, Q.; Zhou, N.; Tian, Y.
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Aspergillus oryzae (W8GG09), Aspergillus oryzae, Aspergillus oryzae JN-412 (W8GG09)
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