Information on EC 3.4.11.5 - prolyl aminopeptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.4.11.5
-
RECOMMENDED NAME
GeneOntology No.
prolyl aminopeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of N-terminal proline from a peptide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-40-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. polyliminolyticus
-
-
Manually annotated by BRENDA team
Brassica oleracea var. capitata
-
-
Manually annotated by BRENDA team
strain CECT12487
-
-
Manually annotated by BRENDA team
strain CECT12487
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Maitake
-
-
Manually annotated by BRENDA team
Maitake
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Lyophyllum cinerascens
-
-
-
Manually annotated by BRENDA team
oral microorganisms
enzyme secreted into saliva
-
-
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
apricot
-
-
Manually annotated by BRENDA team
PAO1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TH-3
-
-
Manually annotated by BRENDA team
strain TH-3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC 35405
-
-
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
-
?
Ala-4-nitroanilide + H2O
L-alanine + p-nitroaniline
show the reaction diagram
Ala-Pro + H2O
L-alanine + L-proline
show the reaction diagram
-
-
-
?
Arg-Pro-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-p-nitroanilide + H2O
glycine + p-nitroaniline
show the reaction diagram
Gly-Pro-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
glycyl-2-naphthylamide + H2O
glycine + 2-naphthylamine
show the reaction diagram
-
6.4% of the activity with L-prolyl-2-naphthylamide
-
-
?
His-p-nitroanilide + H2O
L-histidine + p-nitroaniline
show the reaction diagram
Hyp-Gly + H2O
Hyp + Gly
show the reaction diagram
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
show the reaction diagram
L-alanyl-2-naphthylamide + H2O
L-alanine + 2-naphthylamine
show the reaction diagram
-
6.1% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-arginyl-2-naphthylamide + H2O
L-arginine + 2-naphthylamine
show the reaction diagram
-
3.2% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-histidinyl-2-naphthylamide + H2O
L-histidine + 2-naphthylamine
show the reaction diagram
-
6.3% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
2-naphthylamine + L-hydroxyproline
show the reaction diagram
-
-
-
?
L-hydroxyproline-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
show the reaction diagram
L-hydroxyprolyl-2-naphthylamide + H2O
L-hydroxyproline + 2-naphthylamine
show the reaction diagram
L-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
show the reaction diagram
-
4.7% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-phenylalanyl-2-naphthylamide + H2O
L-phenylalanine + 2-naphthylamine
show the reaction diagram
-
7.6% of the activity with L-prolyl-2-naphthylamide
-
-
?
L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
show the reaction diagram
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
show the reaction diagram
L-Pro-L-Ala + H2O
L-Pro + L-Ala
show the reaction diagram
-
no activity of mutant R136A
-
?
L-Pro-L-Pro-4-(phenylazo)phenylamide + H2O
Pro + 4-phenylazophenylamine
show the reaction diagram
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-proline beta-naphthylamide + H2O
L-proline + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-proline-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
L-prolyl-4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
L-prolyl-p-nitroanilide + H2O
L-proline + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
show the reaction diagram
Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
show the reaction diagram
Leu-Pro-Pro-Ser-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
Lys-4-nitroanilide + H2O
L-lysine + p-nitroaniline
show the reaction diagram
N-L-Pro-2-naphthylamide + H2O
L-proline + naphthylamine
show the reaction diagram
PLSRTLSVAAKK + H2O
LSRTLSVAAKK + L-proline
show the reaction diagram
-
-
-
?
PLSRTLSVAAKK + H2O
Pro + LSRTLSVAAKK
show the reaction diagram
-
-
-
?
poly-(L-Pro) + H2O
proline
show the reaction diagram
-
no hydrolysis
-
-
?
PPGFSPFR + H2O
PGFSPFR + L-proline
show the reaction diagram
-
-
-
?
PPGFSPFR + H2O
Pro + PGFSPFR
show the reaction diagram
-
-
-
?
Pro-2-naphthylamide + H2O
2-naphthylamine + L-proline
show the reaction diagram
-
-
-
?
Pro-2-naphthylamide + H2O
beta-naphthylamine + L-proline
show the reaction diagram
-
-
-
?
Pro-2-naphthylamide + H2O
Pro + 2-naphthylamide
show the reaction diagram
-
-
-
?
Pro-4-nitroanilide + H2O
4-nitroaniline + L-proline
show the reaction diagram
-
-
-
?
Pro-4-nitroanilide + H2O
L-proline + p-nitroaniline
show the reaction diagram
Pro-Ala + H2O
L-alanine + L-proline
show the reaction diagram
-
-
-
?
Pro-Ala + H2O
Pro + Ala
show the reaction diagram
Pro-Asp + H2O
Pro + Asp
show the reaction diagram
-
-
-
-
?
Pro-D-Ala + H2O
Pro + D-Ala
show the reaction diagram
-
-
-
-
?
Pro-D-Phe + H2O
Pro + D-Phe
show the reaction diagram
-
-
-
-
?
Pro-Gly + H2O
Pro + Gly
show the reaction diagram
Pro-Leu + H2O
Pro + Leu
show the reaction diagram
Pro-Leu-Gly + H2O
Leu-Gly + Pro
show the reaction diagram
-
-
-
?
Pro-Leu-Gly-NH2 + H2O
Leu-Gly-NH2 + L-proline
show the reaction diagram
-
-
-
?
Pro-Leu-Gly-NH2 + H2O
Pro + Leu-Gly-NH2
show the reaction diagram
-
-
-
-
?
Pro-Lys + H2O
Pro + Lys
show the reaction diagram
-
-
-
-
?
Pro-p-nitroanilide + H2O
L-proline + p-nitroaniline
show the reaction diagram
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
show the reaction diagram
Pro-p-nitroanilide + H2O
proline + p-nitroaniline
show the reaction diagram
Pro-Phe + H2O
Pro + Phe
show the reaction diagram
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
show the reaction diagram
Pro-Phe-NH2 + H2O
Pro + Phe-NH2
show the reaction diagram
-
-
-
-
?
Pro-Trp + H2O
Pro + Trp
show the reaction diagram
-
-
-
-
?
proline beta-naphthylamide + H2O
proline + beta-naphthylamine
show the reaction diagram
-
-
-
?
proline-7-amido-4-methylcoumarin + H2O
proline + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Val-4-nitroanilide + H2O
L-valine + p-nitroaniline
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bradykinin + H2O
?
show the reaction diagram
M4MBM1
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
?
show the reaction diagram
M4MBM1
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
enhances activity
Mg2+
enhances activity
Ni2+
-
enhances activity
Zn2+
-
inhibits activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinone
-
-
2-mercaptoethanol
1 mM ZnCl2 and 5 mM beta-mercapthoethanol, respectively, relative activity: 61%
4-chloromercuribenzoate
0.1 mM, relative activity: 6%
4-chloromercuribenzoic acid
5,5'-dithiobis(2-nitrobenzoate)
-
-
Al3+
slight inhibition
amastatin
-
0.01 mM
Arphamenine A
-
-
Ba2+
slight inhibition
Bathocuproine
-
inhibitor binds specifically to Cu2+
benzamidine
moderate inhibition
bestatin
beta-mercaptoethanol
-
2 mM
Ca2+
slight inhibition
CuCl2
-
1 mM, 9% residual activity
cysteine
-
2 mM
Diazotized sulfanilic acid
-
-
diethyldicarbonate
Diethylpyrocarbonate
1 mM, relative activity: 3%
diisopropyl fluorophosphate
-
1 mM, 49% residual activity
diphenylcarbamoyl chloride
oral microorganisms
-
enzymes II and III
E-64
-
1 mM, 16% residual activity
ethanol
-
strong inhibitor
Fe3+
slight inhibition
fragment 2-7 of bradykinin
-
1 mM
Heavy metals
-
HgCl2
0.5 mM, relative activity: 31%
hydrochloride
moderate inhibition
iodacetic acid
-
-
iodoacetate
-
2.6% remaining activity at 1 mM
iodoacetic acid
L-Hydroxyprolyl-2-naphthylamide
oral microorganisms
-
competitive
leupeptin
0.04 mM, relative activity: 68%
Mg2+
slight inhibition
Mn2+
strong inhibition
N-ethylmaleimide
N-tosyl-L-lysine chloromethyl ketone
N-tosyl-L-phenylalanyl chloromethyl ketone
0.02 mM, relative activity: 69%
Na+
-
slight inhibition at 2 mM NaCl
o-phenanthroline
-
2 mM
p-bromophenacyl bromide
-
-
p-chloromercuribenzenesulfonate
0.1 mM, relative activity: 0%
p-chloromercuribenzoate
p-chloromercuribenzoic acid
p-hydroxymercuribenzoic acid
-
1 mM, 2% residual activity
PbCl2
-
1 mM, 9% residual activity
phenylmethanesulfonyl fluoride
moderate inhibition
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
prolinol
Lyophyllum cinerascens
-
-
Tetranitromethane
-
-
ZnCl2
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
restores activity after deactivation with p-chloromercuribenzoate
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45 - 2.92
4-acetyloxyproline-beta-naphthylamide
0.34 - 24.2
Ala-p-nitroanilide
0.22
Gly-p-nitroanilide
-
-
0.24
His-p-nitroanilide
-
-
0.84 - 4.27
hydroxyproline-beta-naphthylamide
0.05 - 0.125
Hyp-2-naphthylamide
27.8
Hyp-Gly
-
-
0.83 - 9.3
L-hydroxyproline-2-naphthylamide
0.095 - 0.13
L-Pro-4-nitroanilide
2.07
L-Pro-L-Ala
-
pH 8.0, 37°C, wild-type enzyme
0.101
L-proline-7-amido-4-methylcoumarin
-
3.39
Leu-p-nitroanilide
-
-
11.5
Lys-p-nitroanilide
-
-
0.01 - 1.58
Pro-2-naphthylamide
0.037
Pro-4-nitroanilide
-
0.31 - 2.69
Pro-Ala
0.9
Pro-Asp
-
-
0.78
Pro-D-Ala
-
-
1.86
Pro-D-Phe
-
-
0.71 - 1.79
Pro-Gly
0.31 - 5.3
Pro-Leu
1.85 - 3.6
Pro-Leu-Gly-NH2
1.55
Pro-Lys
-
-
0.04 - 8.29
Pro-p-nitroanilide
0.33 - 1.08
Pro-Phe
1.79
Pro-Phe-Gly-Lys
-
-
0.31
Pro-Phe-NH2
-
-
0.83
Pro-Trp
-
-
0.07 - 1.38
proline beta-naphthylamide
2.15
proline-4-nitroanilide
Vmax: 347.86 micromol/min/mg
0.04
proline-7-amido-4-methylcoumarin
-
pH 7.5, 37°C
8.73
Val-p-nitroanilide
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88 - 84.1
4-acetyloxyproline-2-naphthylamide
2 - 8
Ala-p-nitroanilide
Grifola frondosa
-
-
81.1
Ala-para-nitroanilide
Aneurinibacillus sp.
-
-
7.8
Gly-p-nitroanilide
Grifola frondosa
-
-
6.5
His-p-nitroanilide
Grifola frondosa
-
-
0.017 - 3.9
L-hydroxyproline-2-naphthylamide
16.8
L-Pro-L-Ala
Serratia marcescens
-
pH 8.0, 37°C, wild-type enzyme
213.7
L-proline-7-amido-4-methylcoumarin
Rasamsonia emersonii
Q8X1C7
-
340
Leu-para-nitroanilide
Aneurinibacillus sp.
-
-
26.2
Lys-para-nitroanilide
Aneurinibacillus sp.
-
-
0.03 - 9.7
Pro-2-naphthylamide
160
Pro-p-nitroanilide
Grifola frondosa
-
-
26
Pro-para-nitroanilide
Aneurinibacillus sp.
-
-
0.04 - 9.81
proline beta-naphthylamide
218.1
proline-4-nitroanilide
Phanerochaete chrysosporium
C6KI04
-
12.3
Val-para-nitroanilide
Aneurinibacillus sp.
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2100
L-proline-7-amido-4-methylcoumarin
Rasamsonia emersonii
Q8X1C7
-
40514
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
crude extract, in 50 mM Tris-HCl, pH 7.5, at 37°C
0.0215
-
culture supernatant
0.48
-
type III
0.8
Pro-2-naphthylamide, at 37°C, pH 8.0
1.06
-
purified enzyme
1.43
-
1 mM Pro-p-nitranilide in 0.05 M Tris/HCl, pH 7.5
2.4
substrate: PLSRTLSVAAKK
3.28
-
pH 7.0, 30°C
4.5
substrate: PPGFSPFR
5.13
-
Pro-p-nitroanilide
6.6
PLSRTLSVAAKK, at 30°C, pH 7.5
8.34
4-acetyloxyproline-2-naphthylamide, at 37°C, pH 8.0
8.5
-
pH 7.5, 37°C
10
-
after 700fold purification, in 50 mM Tris-HCl, pH 7.5, at 37°C
18
-
after 835fold purification
18.3
substrate: L-Pro-4-nitroanilide
20.3
substrate: Pro-2-naphthylamide
22.2
substrate: Pro-Leu-Gly
25.7
substrate: Pro-Ala
33.4
Pro-Leu-Gly-NH2, at 30°C, pH 7.5
42.4
substrate: L-hydroxyproline-2-naphthylamide
55.5
PPGFSPFR, at 30°C, pH 7.5
68.3
-
Pro-p-nitroanilide
85.5
Pro-Ala, at 30°C, pH 7.5
191
Lyophyllum cinerascens
-
-
290
Pro-4-nitroanilide, four-fold purified enzyme at 30°C, pH 7.5
780
-
Pro-Leu-NH2
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
no activity below
5.1
-
no activity below
5.2 - 8.8
Lyophyllum cinerascens
-
-
6.5 - 8.5
oral microorganisms
-
-
7.5 - 8
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
inactive above
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
forelimb, hindlimb, cardiac
Manually annotated by BRENDA team
oral microorganisms
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
225
-
gel filtration
30000
-
gel filtration
33000
-
2 * 33000, SDS-PAGRE, 2 * 34090 MALDI-TOF/MS analysis
34090
-
2 * 33000, SDS-PAGRE, 2 * 34090 MALDI-TOF/MS analysis
37620
calculated from cDNA
43000
-
gel filtration
47519
-
6 * 42000, SDS-PAGE, 6 * 47519, calculated
48000
SDS-PAGE analysis reveals two protein bands (51 kDa and 48 kDa)
50600
calculated from cDNA
51000
SDS-PAGE analysis reveals two protein bands (51 kDa and 48 kDa)
53000
-
gel filtration
53500
-
7 * 53500, SDS-PAGE
55000
-
4 * 55000, SDS-PAGE, SDS-PAGE with mercaptoethanol
55400
-
4 * 55400, SDS-PAGE
56000
-
4 * 56000, gel filtration
63000
-
2 * 63000, SDS-PAGE
66000
-
? * 66000, ? * 83000, SDS-PAGE
75000
Lyophyllum cinerascens
-
2 * 75000, SDS-PAGE
83000
-
? * 66000, ? * 83000, SDS-PAGE
100000
120000
150000
Lyophyllum cinerascens
-
gel filtration
180000
-
gel filtration
204000
-
gel filtration
220000
-
gel filtration
250000
-
gel filtration
270000
-
gel filtration
300000
313000
gel filtration
316000
gel filtration of the native enzyme
370000
-
gel filtration
400000
-
gradient gel electrophoresis
550000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34000, SDS-PAGE
heptamer
hexamer
homodimer
homotetramer
-
4 * 50000, SDS-PAGE; 4 * 56000, gel filtration
monomer
tetramer
trimer
-
3 * 34000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme and selenomethionine derivative in the resolution range between 20-2.1 A. Space group P212121
hanging drop vapor diffusion
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
-
-
664354
5 - 8
highest stability found between pH 6 an 7
666365
5 - 9
-
-
683184
6.5 - 7.5
-
-
35946
6.5 - 8
-
overnight at 4°C
35947
7.25 - 9
-
-
35945
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
significant activity decrease at 50°C
36 - 75
-
complete loss of activity at 75°C
37
-
30 min, stable up to
55
-
inactivation above
65
-
more than 60% activity remained
80
-
inactivation
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
methylene blue or rose bengal, photooxidation
-
35947
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 50% v/v glycerol
-
-20°C or 4°C
-
-20°C, 50% v/v glycerol, at least 6 months
-
4°C, 8 weeks
oral microorganisms
-
4°C, in 50 mM Tris-HCl buffer at pH 7.5, several months, no loss of activity
-
4°C, in phosphate buffer between pH 7.5 and 8.5, overnight, remains stable
-
4°C, in the absence of protective reagents, 3 days, little or no activity remains
-
4°C, purified enzyme, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 enzymes, II and III specific for naphthylamides of L-Pro and L-Hyp
oral microorganisms
-
ammonium sulfate fractionation, Toyopearl QAE-550C column chromatography, Sephadex G-200 gel filtration, and Mono Q column chromatography
-
chromatography
-
column chromatography
DEAE Sepharose CL6B, Butyl-Toyopearl, Sephacryl S-100 and Mono-Q column chromatographies
-
enzyme is partially purified through two-step column chromatography using a Ni-IMAC column and a MonoQ column
expressed in Escherichia coli
four chromatography steps
partial
-
partial, 3 enzymes: I, II, III
-
purified to homogeneity by ammonium sulfate fractionation followed by five successive chromatographic steps
recombinant wild-type and mutant enzymes from Escherichia coli
-
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 as a His-tagged fusion protein
-
expressed in Lactobacillus casei strain. The strain successfully survives 12 weeks of ripening period in cheese. The food-grade plasmid carrying the pepI gene, is stable and PepI enzyme is active in LAB6 cells isolated at different stages of the ripening process
-
expression in Escherichia coli
expression in Escherichia coli. Enzyme carrying a C-terminal His-tag is less stable than native enzyme
-
expression of wild-type and mutants in Escherichia coli
-
in a reporter plasmids, one of the two consecutive S-layer protein (slpA) promoters (P1, P2) is placed upstream of the Lactobacillus helveticus proline iminopeptidase gene, and defined parts of the sequences upstream of the promoter are deleted. Reporter plasmid is expressed in Lactobacillus lactis and reporter gene expression is determined
PAP is overexpressed as a His-tag fusion protein under a taka-amylase gene (amyB) promoter with a limited expressing condition in Aspergillus oryzae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in plants grown on nutrient media supplemented with NaCl or metal ions (such as cadmium and aluminium ions) in the nutrient medium, a considerable increase in the expression of TsPAP1 is observed; under drought conditions, a significant 2.5fold increase in the TsPAP1 transcript level is observed as early as the first day after the stress application
-
Northern analysis indicates that Tepap mRNA levels are regulated by the composition of the growth medium. Highest Tepap transcript levels are observed when the fungus is grown in medium containing glucose and the protein hydrolysate casitone
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264A
mutant shows no enzymatic activity
H292L
mutant shows no enzymatic activity
S107D
mutant shows no enzymatic activity
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
nutrition
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