3.4.11.5: prolyl aminopeptidase
This is an abbreviated version!
For detailed information about prolyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.5
-
3.4.11.5
-
women
-
cervical
-
smear
-
cytology
-
pulmonary
-
artery
-
intraepithelial
-
colposcopy
-
neoplasia
-
hypertension
-
cervix
-
services
-
high-risk
-
high-grade
-
hemodynamic
-
mammography
-
undetermined
-
physician
-
low-grade
-
demographic
-
airway
-
attend
-
dysplasia
-
vaginal
-
gynecologic
-
bethesda
-
insurance
-
triage
-
apnea
-
precancerous
-
endocervical
-
exam
-
hysterectomy
-
mammogram
-
catheterization
-
medicine
-
food industry
-
atypia
-
cytopathology
-
industry
-
biotechnology
-
agriculture
-
low-income
-
nutrition
-
peroxidase-antiperoxidase
-
marital
-
hpv-positive
-
receipt
-
polysomnography
-
intercourse
-
self-efficacy
-
medicaid
-
sociodemographic
-
analysis
-
sleepiness
-
telephone
-
married
- 3.4.11.5
- women
- cervical
-
smear
-
cytology
- pulmonary
- artery
-
intraepithelial
-
colposcopy
- neoplasia
- hypertension
- cervix
-
services
-
high-risk
-
high-grade
-
hemodynamic
-
mammography
-
undetermined
-
physician
-
low-grade
-
demographic
- airway
-
attend
- dysplasia
- vaginal
- gynecologic
-
bethesda
-
insurance
-
triage
- apnea
-
precancerous
- endocervical
-
exam
-
hysterectomy
-
mammogram
-
catheterization
- medicine
- food industry
-
atypia
-
cytopathology
- industry
- biotechnology
- agriculture
-
low-income
- nutrition
-
peroxidase-antiperoxidase
-
marital
-
hpv-positive
-
receipt
-
polysomnography
-
intercourse
-
self-efficacy
-
medicaid
-
sociodemographic
- analysis
- sleepiness
-
telephone
-
married
Reaction
release of N-terminal proline from a peptide =
Synonyms
aminopeptidase P, aminopeptidase, proline, APP, cytosol aminopeptidase V, EC 3.4.1.4, L-proline aminopeptidase, L-prolyl-peptide hydrolase, More, pamA, PAP, PchPiPA, PepI, pepIP, PEPP, Pf S33 proline aminopeptidase, PfPAP, PIP, PiPA, Plasmodium falciparum S33 proline aminopeptidase, Pro-X aminopeptidase, proline aminopeptidase, proline iminopeptidase, proline-specific aminopeptidase, Prolyl aminopeptidase, TaPAP1, TePAP, Tricorn protease interacting factor F1, TsPAP1, X-pro aminopeptidase (Lactococcus)
ECTree
3.4.11.5 prolyl aminopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.11.5 - prolyl aminopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-acetyloxyproline-2-naphthylamide + H2O
2-naphthylamine + 4-acetyloxyproline
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + beta-naphthylamine
-
-
-
?
glycyl-2-naphthylamide + H2O
glycine + 2-naphthylamine
-
6.4% of the activity with L-prolyl-2-naphthylamide
-
-
?
Hyp-beta-naphthylamide + H2O
Hyp + beta-naphthylamine
-
-
-
?
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-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
-
4.7% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-phenylalanyl-2-naphthylamide + H2O
L-phenylalanine + 2-naphthylamine
-
7.6% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
-
-
-
?
L-Pro-L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
-
-
-
?
L-proline beta-naphthylamide + H2O
L-proline + 2-naphthylamine
-
-
-
?
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
-
-
?
Pro-7-amido-4-methylcoumarin + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
Pro-Gly-Gly + H2O
Pro + Gly-Gly
low activity
-
-
?
Pro-Gly-Gly-Gly + H2O
Pro + Gly-Gly-Gly
low activity
-
-
?
Pro-Leu-Gly + H2O
Pro + Leu-Gly
low activity
-
-
?
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
-
-
?
proline beta-naphthylamide + H2O
proline + beta-naphthylamine
-
-
-
?
proline-7-amido-4-methylcoumarin + H2O
proline + 7-amino-4-methylcoumarin
-
-
-
?
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-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-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-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
-
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
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
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
-
influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis
-
-
?
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
-
-
?
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
Lacticaseibacillus rhamnosus NCDC 347
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Lactiplantibacillus plantarum ATCC BAA-793
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Lactiplantibacillus plantarum NCDC 020
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Lactiplantibacillus plantarum NCIMB 8826
-
-
-
?
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
Lactobacillus acidophilus NCDC 013
-
-
-
?
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
Levilactobacillus brevis JCM 1170
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Levilactobacillus brevis NCDC 371
-
-
-
?
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
Limosilactobacillus fermentum NCDC 406
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
Loigolactobacillus coryniformis NCDC 366
-
-
-
-
?
Pro-4-methoxy-beta-naphythylamide + H2O
Pro + 4-methoxy-beta-naphythylamine
-
-
-
?
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
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-Leu + H2O
Pro + Leu
69.5% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Leu + H2O
Pro + Leu
low activity
-
-
?
Pro-Lys + H2O
Pro + Lys
74.4% activity compared to Pro-Phe-Gly-Lys
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
best peptide substrate
-
-
?
Pro-Pro + H2O
Pro + Pro
44.1% activity compared to Pro-Phe-Gly-Lys
-
-
?
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
?
-
Aspergillus oryzae JN-412
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
?
-
Aspergillus oryzae JN-412
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
?
-
Lacticaseibacillus rhamnosus NCDC 347
the enzyme is a serine protease
-
-
?
additional information
?
-
the enzyme is a serine protease
-
-
?
additional information
?
-
-
the enzyme is a serine protease
-
-
?
additional information
?
-
Lactiplantibacillus plantarum ATCC BAA-793
the enzyme is a serine protease
-
-
?
additional information
?
-
Lactiplantibacillus plantarum NCDC 020
the enzyme is a serine protease
-
-
?
additional information
?
-
Lactiplantibacillus plantarum NCIMB 8826
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
?
-
Limosilactobacillus fermentum NCDC 406
the enzyme is a serine protease
-
-
?
additional information
?
-
-
the enzyme is a serine protease
-
-
?
additional information
?
-
Loigolactobacillus coryniformis NCDC 366
-
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
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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
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additional information
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substrate specificity and binding mechanism
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