Information on EC 3.4.99.B2 - D-aspartyl endopeptidase

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

EC NUMBER
COMMENTARY hide
3.4.99.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
D-aspartyl endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side
show the reaction diagram
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-
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Caenorhabditis elegans
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
strain B38
-
-
Manually annotated by BRENDA team
strain B38
-
-
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
D-Asp-L-Ala-L-Glu-L-Phe-L-Arg-L-His-D-Asp-L-Ser-Gly-L-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
DAEFRH-(D-Asp)-GSY + H2O
DAEFRH-(D-Asp) + GSY
show the reaction diagram
L-Thr-L-Val-L-Leu-D-alpha-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-D-Asp-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
succinyl-D-Asp-7-amido-4-methylcoumarin + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-D-Asp-alpha-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-D-Asp-p-nitroanilide + H2O
succinyl-D-Asp + p-nitroaniline
show the reaction diagram
[D-Asp]AEFRH[D-Asp]SGY + H2O
[D-Asp]AEFRHX + SGY
show the reaction diagram
-
the D-Abeta1-10 peptide is degraded at D-Asp7 and two peptides are produced [D-Asp]AEFRHX and SGY. X is not identified in this study. L-Abeta1–10 peptide could not be degraded by this enzyme
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-
?
[D-Asp]AEFRH[D-Asp]SGY + H2O
[D-Asp]AEFRH[D-Asp] + SGY
show the reaction diagram
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the D-Abeta1-10 peptide is degraded at D-Asp7 and two peptides are produced [D-Asp]AEFRHX and SGY. X is not identified in this study. L-Abeta1–10 peptide could not be degraded by this enzyme
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?
additional information
?
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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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme is independent of ATP or NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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3 mM, activity is increased by a factor of two
Ca2+
-
3 mM, activity is increased by a factor of two
Mg2+
-
3 mM, activity is increased by a factor of two
Mn2+
-
3 mM, activity is increased by a factor of two
Sr2+
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3 mM, activity is increased by a factor of two
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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0.1 mM, 8.3% inhibition
Aprotinin
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0.1 mM, 14% inhibition
benzoyl-Arg-His-D-Asp-CH2Cl
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1 mM, about 70% inhibition of paenidase I and II
benzoyl-L-Arg-L-His-D-Asp-CH2Cl
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0.003 mM, 50% inhibition
biotinyl-(epsilon-aminocaproic acid)-L-Arg-L-His-D-Asp-CH2Cl
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-
Co2+
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1.0 mM, 31% inhibition of paenidase I, 46% inhibition of paenidase II
diisopropyl fluorophosphate
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at 0.5 mM, 15.5% inhibition
lactacystin
leupeptin
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0.03 mM, 8.5% inhibition
Mn2+
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1.0 mM MnCl2, 31% inhibition of paenidase I, 60% inhibition of paenidase II
NEM
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0.1 mM, about 10% inhibition
Pepstatin
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0.01 mg/ml, about 50% inhibition of paenidase I and II
pepstatin A
phosphoramidon
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0.01 mM, 9.9% inhibition
Zn2+
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0.25 mM ZnCl2, 98% inhibition of paenidase I and II
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1.25
succinyl-D-Asp-4-methylcoumaryl-7-amide
0.12
succinyl-D-Asp-alpha-4-methylcoumaryl-7-amide
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pH 8,5, 37°C
1.03 - 1.26
succinyl-D-Asp-p-nitroanilide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.66 - 1.93
succinyl-D-Asp-4-methylcoumaryl-7-amide
4.7 - 6.6
succinyl-D-Asp-p-nitroanilide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
benzoyl-L-Arg-L-His-D-Asp-CH2Cl
Oryctolagus cuniculus
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pH 8.5, 37°C
0.15
lactacystin
Oryctolagus cuniculus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2370
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paenidase II
2880
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paenidase I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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paenidases I and II, succinyl-D-Asp-4-methylcoumaryl-7-amide or succinyl-D-Asp-p-nitroanilide as a substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
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pH 7: about 80% of maximal activity, pH 9.0: about 60% of maximal activity, paenidases I and II, succinyl-D-Asp-4-methylcoumaryl-7-amide as substrate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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weak activity
Manually annotated by BRENDA team
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moderate activity
Manually annotated by BRENDA team
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weak activity
Manually annotated by BRENDA team
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weak activity
Manually annotated by BRENDA team
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weak activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
inner mitochondrial membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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1 * 33000, paenidase II lacks 5 of the residues present in the N-terminal sequence of paenidase I, paenidase II
34000
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1 * 34000, paenidase I
34170
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paenidase II, paenidase II lacks 5 of the residues present in the N-terminal sequence of paenidase I, MALDI-TOF/MS
34790
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paenidase I, MALDI-TOF/MS
35000
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gel filtration
600000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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pH 8, 30 min, stable below, paenidases I and II
40
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pH 8, 30 min, paenidase I: about 20% loss of activity, paenidase II: about 30% loss of activity
50
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pH 8, 30 min, about 40% loss of activity, paenidases I and II
60
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pH 8, 30 min, paenidase I: about 80% loss of activity, paenidase II: about 90% loss of activity
70
-
pH 8, 30 min, complete loss of activity, paenidases I and II
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
paenidases I and II
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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a system for screening D-Asp-containing proteins is developed by using D-aspartyl endopeptidase and a two-dimensional gel electrophoresis