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Information on EC 3.4.19.5 - beta-aspartyl-peptidase and Organism(s) Escherichia coli and UniProt Accession P37595

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.5 beta-aspartyl-peptidase
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This record set is specific for:
Escherichia coli
UNIPROT: P37595 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
Synonyms
ntn-hydrolase, isoaspartyl dipeptidase, hasrgl1, cpsiada, asparaginase-like protein 1, isoaspartyl peptidase/l-asparaginase, beta-aspartyl peptidase, isoaspartyl peptidase, isoaspartyl aminopeptidase/asparaginase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
asparaginase
-
isoaspartyl aminopeptidase
-
beta-aspartyl dipeptidase
-
-
-
-
beta-aspartyl peptidase
-
-
-
-
dipeptidase, beta-aspartyl
-
-
-
-
isoaspartyl dipeptidase
-
isoaspartyl peptidase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-74-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-Asp-Leu + H2O
L-Asp + L-Leu
show the reaction diagram
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
show the reaction diagram
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
show the reaction diagram
-
-
-
?
beta-Asp-His + H2O
Asp + His
show the reaction diagram
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
show the reaction diagram
beta-Asp-Lys + H2O
Asp + Lys
show the reaction diagram
-
-
-
?
beta-Asp-Phe + H2O
Asp + Phe
show the reaction diagram
-
-
-
?
iso-Asp-Gly + H2O
?
show the reaction diagram
-
-
-
?
iso-Asp-Leu + H2O
?
show the reaction diagram
best substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
does not appear to be involved in glutathione metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Asp-PSI[PO2CH2]-LeuOH
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
alpha-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
3.7
beta-Asp-Ala
wild-type enzyme, pH 8.1, 30°C
18
beta-Asp-Gly
wild-type enzyme, pH 8.1, 30°C
3.7
beta-Asp-His
wild-type enzyme, pH 8.1, 30°C
0.09 - 34
beta-Asp-Leu
0.91
beta-Asp-Lys
wild-type enzyme, pH 8.1, 30°C
0.23
beta-Asp-Phe
wild-type enzyme, pH 8.1, 30°C
0.8
beta-aspartyl-L-leucine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.7
alpha-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
213
beta-Asp-Ala
wild-type enzyme, pH 8.1, 30°C
0.93
beta-Asp-Gly
wild-type enzyme, pH 8.1, 30°C
20.8
beta-Asp-His
wild-type enzyme, pH 8.1, 30°C
0.00062 - 104
beta-Asp-Leu
58
beta-Asp-Lys
wild-type enzyme, pH 8.1, 30°C
16.9
beta-Asp-Phe
wild-type enzyme, pH 8.1, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
SDS-PAGE, intact precursor molecule, 19000 + 14000 (native protein) after autoproteolysis
320000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
the enzyme is dimer of heterodimers (alphabeta)2
additional information
the quarternary structure of the enzyme is octameric and can be described as a tetramer od dimers. Each subunit folds into two distinct domains
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, 1.9 A resolution
hanging drop method of vapor diffusion, the best crystals are observed growing at 25°C from 10% poly(ethylene glycol)8000, 100 mM homopipes, pH 5, in the presence of MgCl2
-
hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His
hanging-drop vapour-diffusion method, crystal structure of EcAIII at 1.65 A resolution
-
sitting drop vapor diffusion method, crystal structure in the absence and presence of the phosphinic inhibitor Asp-PSI[PO2CH2]-LeuOH
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T179A
does not undergo autoprocessing
D285A
kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value
D285N
kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value
E77D
kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value
E77Q
kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value
R169K
kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value
R169M
kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value
R233K
kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value
R233M
kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value
S289A
kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value
Y137A
kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value
Y137F
kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gary, J.D.; Clarke, S.
Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli
J. Biol. Chem.
270
4076-4087
1995
Escherichia coli
Manually annotated by BRENDA team
Jozic, D.; Kaiser, J.T.; Huber, R.; Bode, W.; Maskos, K.
X-ray Structure of isoaspartyl dipeptidase from E. coli: a dinuclear zinc peptidase evolved from amidohydrolases
J. Mol. Biol.
332
243-256
2003
Escherichia coli (P39377)
Manually annotated by BRENDA team
Thoden, J.B.; Marti-Arbona, R.; Raushel, F.M.; Holden, H.M.
High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli
Biochemistry
42
4874-4882
2003
Escherichia coli
Manually annotated by BRENDA team
Prahl, A.; Pazgier, M.; Hejazi, M.; Lockau, W.; Lubkowski, J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli
Acta Crystallogr. Sect. D
D60
1173-1176
2004
Escherichia coli
Manually annotated by BRENDA team
Marti-Arbona, R.; Fresquet, V.; Thoden, J.B.; Davis, M.L.; Holden, H.M.; Raushel, F.M.
Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli
Biochemistry
44
7115-7124
2005
Escherichia coli (P39377), Escherichia coli
Manually annotated by BRENDA team
Michalska, K.; Brzezinski, K.; Jaskolski, M.
Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate
J. Biol. Chem.
280
28484-28491
2005
Escherichia coli (P37595), Escherichia coli
Manually annotated by BRENDA team
Michalska, K.; Hernandez-Santoyo, A.; Jaskolski, M.
The mechanism of autocatalytic activation of plant-type L-asparaginases
J. Biol. Chem.
283
13388-13397
2008
Escherichia coli (P37595)
Manually annotated by BRENDA team
Zhang, H.M.; Chen, S.L.
Include dispersion in quantum chemical modeling of enzymatic reactions the case of isoaspartyl dipeptidase
J. Chem. Theory Comput.
11
2525-2535
2015
Escherichia coli (P39377), Escherichia coli K12 (P39377)
Manually annotated by BRENDA team