Information on EC 3.4.19.5 - beta-aspartyl-peptidase

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

EC NUMBER
COMMENTARY hide
3.4.19.5
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RECOMMENDED NAME
GeneOntology No.
beta-aspartyl-peptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-74-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme from human faeces, present in healthy individuals, absent in antibiotic-treated patients
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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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
alpha-Asp-Leu + H2O
L-Asp + L-Leu
show the reaction diagram
-
-
-
-
?
Asp-Gly-Ala + H2O
Asp + Gly-Ala
show the reaction diagram
-
55% of the activity with beta-aspartylglycine
-
?
Asp-Gly-Val + H2O
Asp + Gly-Val
show the reaction diagram
-
13% of the activity with beta-aspartylglycine
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?
beta-Asp-Ala + H2O
Asp + Ala
show the reaction diagram
beta-Asp-Gln + H2O
Asp + Gln
show the reaction diagram
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
show the reaction diagram
beta-Asp-Gly-Gly + H2O
Asp + Gly-Gly
show the reaction diagram
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95% of the activity with beta-aspartylglycine
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?
beta-Asp-His + H2O
Asp + His
show the reaction diagram
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-
-
-
?
beta-Asp-Ile + H2O
Asp + Ile
show the reaction diagram
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37% of the activity with beta-aspartylglycine
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?
beta-Asp-Leu + H2O
Asp + Leu
show the reaction diagram
beta-Asp-Lys + H2O
Asp + Lys
show the reaction diagram
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-
-
-
?
beta-Asp-Met + H2O
Asp + Met
show the reaction diagram
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82% of the activity with beta-aspartylglycine
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?
beta-Asp-Phe + H2O
Asp + Phe
show the reaction diagram
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-
-
-
?
beta-Asp-Phe + H2O
L-Asp + L-Phe
show the reaction diagram
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-
-
?
beta-Asp-Ser + H2O
Asp + Ser
show the reaction diagram
beta-Asp-Thr + H2O
Asp + Thr
show the reaction diagram
-
29% of the activity with beta-aspartylglycine
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?
beta-Asp-Val + H2O
Asp + Val
show the reaction diagram
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28% of the activity with beta-aspartylglycine
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?
beta-L-Asp-L-Ala + H2O
L-Asp + L-Ala
show the reaction diagram
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-
-
?
beta-L-Asp-L-Leu + H2O
L-Asp + L-Leu
show the reaction diagram
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-
-
?
beta-L-Asp-L-Lys + H2O
L-Asp + L-Lys
show the reaction diagram
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-
-
?
beta-L-Asp-L-Phe + H2O
L-Asp + L-Phe
show the reaction diagram
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-
-
?
beta-L-Asp-L-Phe methyl ester + H2O
L-Asp + L-Phe methyl ester
show the reaction diagram
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-
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?
iso-Asp-Gly + H2O
?
show the reaction diagram
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?
iso-Asp-Leu + H2O
?
show the reaction diagram
best substrate
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?
L-Asp beta-methyl ester + H2O
L-Asp + methanol
show the reaction diagram
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?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
L-aspartic acid + 7-amino-4-methylcoumarin
show the reaction diagram
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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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does not appear to be involved in glutathione metabolism
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the active site consists of a binuclear metal center positioned at the C-terminal end of a (beta/alpha)8-barrel domain
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Asp-PSI[PO2CH2]-LeuOH
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p-hydroxymercuribenzoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
alpha-Asp-Leu
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wild-type enzyme, pH 8.1, 30C
3.7
beta-Asp-Ala
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wild-type enzyme, pH 8.1, 30C
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18
beta-Asp-Gly
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wild-type enzyme, pH 8.1, 30C
3.7
beta-Asp-His
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wild-type enzyme, pH 8.1, 30C
0.09 - 34
beta-Asp-Leu
0.91
beta-Asp-Lys
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wild-type enzyme, pH 8.1, 30C
0.23 - 0.41
beta-Asp-Phe
0.8
beta-aspartyl-L-leucine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.7
alpha-Asp-Leu
Escherichia coli
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wild-type enzyme, pH 8.1, 30C
213
beta-Asp-Ala
Escherichia coli
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wild-type enzyme, pH 8.1, 30C
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0.93
beta-Asp-Gly
Escherichia coli
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wild-type enzyme, pH 8.1, 30C
20.8
beta-Asp-His
Escherichia coli
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wild-type enzyme, pH 8.1, 30C
0.00062 - 104
beta-Asp-Leu
58
beta-Asp-Lys
Escherichia coli
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wild-type enzyme, pH 8.1, 30C
1.98 - 16.9
beta-Asp-Phe
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.83
beta-Asp-Phe
Cavia porcellus
H0VQC8
pH 7.5, 37C
35931
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
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Tris-HCl buffer
7.4
assay at
7.5 - 8
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sodium phosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14550
mass spectroscopy, beta-subunit
15000
beta-subunit, SDS-PAGE
18000
Western blot, reducing conditions, detected in soluble and insoluble fractions
18500
mass spectroscopy, alpha-subunit
20000
alpha-subunit, SDS-PAGE
33020
mass spectroscopy, precursor enzyme
35000
inactive precursor, SDS-PAGE
320000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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the enzyme is dimer of heterodimers (alphabeta)2
additional information
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the quarternary structure of the enzyme is octameric and can be described as a tetramer od dimers. Each subunit folds into two distinct domains
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
inactive precursor undergoes a self-activation process, converting it from an uncleaved precursor of 35000 Da into alpha- and beta-subunits of 20000 and 15000 Da, respectively. Glycine stimulates cleavage in a dose-dependent manner
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
uncleaved (inactive) as well as the cleaved (active), aspartate-bound structures. Cleavage does not greatly alter the overall structure of the enzyme with the exception of the conformational change in the conserved HGG loop that coincides with cleavage
hanging drop method of vapor diffusion, the best crystals are observed growing at 25C from 10% poly(ethylene glycol)8000, 100 mM homopipes, pH 5, in the presence of MgCl2
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hanging drop vapor diffusion method, 1.9 A resolution
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hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His
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hanging-drop vapour-diffusion method, crystal structure of EcAIII at 1.65 A resolution
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sitting drop vapor diffusion method, crystal structure in the absence and presence of the phosphinic inhibitor Asp-PSI[PO2CH2]-LeuOH
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability is dependent on the presence of sodium ions
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stable to freezing and thawing in 0.01 M sodium phosphate buffer
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unstable to dialysis against water or 0.01 M Tris-HCl buffer, pH 8.0, if 0.01 M NaCl is included in the dialysis solution, 80% of the activity is recovered
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, stable for 5 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography. hASRGL1 purification by immobilized metal ion affinity chromatography yields 30 mg of protein/l with a purity of more than 90% as determined by SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein in Escherichia coli
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D285A
-
kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value
D285N
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kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value
E77D
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kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value
E77Q
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kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value
R169K
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kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value
R169M
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kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value
R233K
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kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value
R233M
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kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value
S289A
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kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value
T179A
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does not undergo autoprocessing
Y137A
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kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value
Y137F
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kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value
T168A
mutant does not show enzymatic activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
isoform ASRGL1 is not the asparaginase responsible for the antitumor effects elicited by treatment with guinea pig serum
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