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Information on EC 3.4.11.5 - prolyl aminopeptidase and Organism(s) Serratia marcescens and UniProt Accession O32449

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.5 prolyl aminopeptidase
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This record set is specific for:
Serratia marcescens
UNIPROT: O32449 not found.
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Word Map
The taxonomic range for the selected organisms is: Serratia marcescens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of N-terminal proline from a peptide
Synonyms
pap, aminopeptidase p, proline iminopeptidase, prolyl aminopeptidase, proline aminopeptidase, pepip, tspap1, proline-specific aminopeptidase, tepap, l-proline aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proline iminopeptidase
-
Prolyl aminopeptidase
-
aminopeptidase, proline
-
-
-
-
cytosol aminopeptidase V
L-proline aminopeptidase
-
-
-
-
L-prolyl-peptide hydrolase
-
-
-
-
PAP
-
-
-
-
PIP
-
-
-
-
Pro-X aminopeptidase
proline aminopeptidase
proline iminopeptidase
-
PIP
Prolyl aminopeptidase
Tricorn protease interacting factor F1
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of N-terminal proline from a peptide
show the reaction diagram
substrate recognition mechanism, Phe139 and Glu204 recognize the pyrrolidine ring and the amino group of proline at the S1 site, Arg136 recognizes the P'1 site
-
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
9025-40-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-acetyloxyproline-2-naphthylamide + H2O
2-naphthylamine + 4-acetyloxyproline
show the reaction diagram
-
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
2-naphthylamine + L-hydroxyproline
show the reaction diagram
-
-
-
?
L-hydroxyprolyl-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
show the reaction diagram
-
-
-
?
Pro-2-naphthylamide + H2O
beta-naphthylamine + L-proline
show the reaction diagram
-
-
-
?
L-Pro-L-Ala + H2O
L-Pro + L-Ala
show the reaction diagram
-
no activity of mutant R136A
-
?
L-prolyl-peptide + H2O
L-proline + peptide
show the reaction diagram
-
-
-
-
?
proline beta-naphthylamide + H2O
proline + beta-naphthylamine
show the reaction diagram
-
-
-
?
additional information
?
-
-
substrate specificity and binding mechanism
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoic acid
-
-
heavy metals
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45 - 2.92
4-acetyloxyproline-beta-naphthylamide
0.84 - 4.27
hydroxyproline-beta-naphthylamide
0.83 - 9.3
L-hydroxyproline-2-naphthylamide
0.42 - 1.58
Pro-2-naphthylamide
2.07
L-Pro-L-Ala
-
pH 8.0, 37°C, wild-type enzyme
0.07 - 1.38
proline beta-naphthylamide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88 - 84.1
4-acetyloxyproline-2-naphthylamide
0.017 - 3.9
L-hydroxyproline-2-naphthylamide
0.03 - 9.7
Pro-2-naphthylamide
16.8
L-Pro-L-Ala
-
pH 8.0, 37°C, wild-type enzyme
0.04 - 9.81
proline beta-naphthylamide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
L-hydroxyproline-2-naphthylamide, at 37°C, pH 8.0
0.8
Pro-2-naphthylamide, at 37°C, pH 8.0
8.34
4-acetyloxyproline-2-naphthylamide, at 37°C, pH 8.0
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PIP_SERMA
317
0
36084
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme structure, active site structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
column chromatography
recombinant wild-type and mutant enzymes from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression of wild-type and mutants in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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cheese ripening, debittering, milk processing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshimoto, T.; Kabashima, T.; Uchikawa, K.; Inoue, T.; Tanaka, N.; Nakamura, K.T.; Tsuru, M.; Ito, K.
Crystal structure of prolyl aminopeptidase from Serratia marcescens
J. Biochem.
126
559-565
1999
Serratia marcescens
Manually annotated by BRENDA team
Ito, K.; Inoue, T.; Kabashima, T.; Kanada, N.; Huang, H.S.; Ma, X.; Azmi, N.; Azab, E.; Yoshimoto, T.
Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens
J. Biochem.
128
673-678
2000
Serratia marcescens
Manually annotated by BRENDA team
Kitazono, A.A.; Ito, K.; Yoshimoto, T.
CLAN SC - S33 604. Prolyl aminopeptidase
Handbook of proteolytic enzymes, (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2nd. Ed.
1943-1947
2004
Aeromonas sobria, Weizmannia coagulans, Elizabethkingia meningoseptica, Hafnia alvei, Lactobacillus delbrueckii, Neisseria gonorrhoeae, Serratia marcescens, Thermoplasma acidophilum, Xanthomonas campestris
-
Manually annotated by BRENDA team
Nakajima, Y.; Ito, K.; Sakata, M.; Xu, Y.; Nakashima, K.; Matsubara, F.; Hatakeyama, S.; Yoshimoto, T.
Unusual extra space at the active site and high activity for acetylated hydroxyproline of prolyl aminopeptidase from Serratia marcescens
J. Bacteriol.
188
1599-1606
2006
Serratia marcescens (O32449), Serratia marcescens
Manually annotated by BRENDA team