Information on EC 3.4.11.19 - D-stereospecific aminopeptidase

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

EC NUMBER
COMMENTARY hide
3.4.11.19
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RECOMMENDED NAME
GeneOntology No.
D-stereospecific aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal D-amino acid from a peptide, Xaa-/-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides and methyl esters also are hydrolysed, as is glycine amide
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
57534-78-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
dppA gene product
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
no significant differences are observed in the vegetative growth and conidiation on minimal and complete media in the enzyme gene disruptant or overexpression strains
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-aminobutanamide + H2O
(R)-2-aminobutanoic acid + NH3
show the reaction diagram
D-2-aminobutyric acid amide + H2O
D-aminobutyric acid + NH3
show the reaction diagram
D-Ala 4-nitroanilide + H2O
D-Ala + 4-nitroaniline
show the reaction diagram
D-Ala-3-aminopentane amide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
show the reaction diagram
D-Ala-D-Ala + H2O
D-Ala
show the reaction diagram
D-Ala-Gly + H2O
D-Ala + Gly
show the reaction diagram
D-Ala-Gly-Gly + H2O
D-Ala + Gly-Gly
show the reaction diagram
D-Ala-L-Ala-L-Ala + H2O
D-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
D-Ala4 + H2O
?
show the reaction diagram
-
-
-
-
?
D-alanine amide + H2O
D-Ala + NH3
show the reaction diagram
D-alanine benzylamide + H2O
D-Ala + benzylamine
show the reaction diagram
-
-
-
-
?
D-alanine n-butylamide + H2O
D-Ala + n-butylamine
show the reaction diagram
-
-
-
-
?
D-serine amide + H2O
D-serine + NH3
show the reaction diagram
D-threonine amide + H2O
D-Thr + NH3
show the reaction diagram
-
-
-
-
?
fluoresceyl-Gly-6-aminopenicillanic acid + H2O
?
show the reaction diagram
-
penicillin-binding activity of mutant lacking residues 476-486
-
-
?
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
?
Gly-L-Ala + H2O
Gly + L-Ala
show the reaction diagram
-
-
-
?
Gly-L-Cys + H2O
Gly + L-Cys
show the reaction diagram
-
-
-
?
glycine amide + H2O
Gly + NH3
show the reaction diagram
-
-
-
-
?
L-2-aminobutyric amide + H2O
D-2-aminobutyric acid + NH3
show the reaction diagram
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in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
-
-
?
L-Ala 4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
12% of the activity with Gly 4-nitroanilide
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-
?
L-Ala-D-Ala + H2O
L-Ala + D-Ala
show the reaction diagram
-
-
-
?
L-alanine amide + H2O
D-alanine + NH3
show the reaction diagram
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in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
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-
?
L-methionine amide + H2O
D-methionine + NH3
show the reaction diagram
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in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
-
-
?
L-serine amide + H2O
D-serine + NH3
show the reaction diagram
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in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
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-
?
Nalpha, Nalpha-Ac2-L-Lys-D-Ala-D-Ala + H2O
Nalpha, Nalpha-Ac2-L-Lys-D-Ala + D-Ala
show the reaction diagram
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wild-type, no substrate. Mutant lacking residues 476-486 with or without mutation N275R, small D,D-carboxypeptidase activity
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-
?
Nalpha-Ac-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Ac-L-Lys-D-Ala + D-Ala
show the reaction diagram
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wild-type and mutant lacking residues 476-486, no substrate. Mutant lacking residues 476-486 plus mutation N275R, small D,D-carboxypeptidase activity
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-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5,5'-dithiobis(2-nitrobenzoic acid)
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6-aminopenicillanic acid
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7-aminocephalosporanic acid
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AEBSF
1 mM, 45% residual activity
ampicillin
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benzylpenicillin
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Co2+
1 mM, 50% residual activity
hydroxylamine
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NaCl
1 M, 40% residual activity
nitrocefin
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inhibitory on D,D-carboxypeptidase activity of mutant lacking residues 476-486 plus mutation N275R
additional information
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probably has serine at the active centre, not: EDTA (0.2 mM)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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additional information
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thiol-dependent
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.3
D-2-Aminobutyric acid amide
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-
0.33
D-Ala 4-nitroanilide
pH 9.0, 30°C
0.51
D-Ala benzylamide
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-
2.27
D-Ala-3-aminopentane amide
-
-
0.46 - 5.1
D-Ala-4-nitroanilide
10.2
D-Ala-D-Ala
-
-
0.57
D-Ala-D-Ala-D-Ala
-
-
0.98
D-Ala-Gly
-
-
0.37
D-Ala-Gly-Gly
-
-
1.03
D-Ala-L-Ala
-
-
0.65
D-Ala-L-Ala-L-Ala
-
-
0.73
D-Ala-n-butylamide
-
-
0.32
D-Ala4
-
-
0.65
D-Alanine amide
-
-
0.51
D-alanine-4-nitroanilide
-
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27
D-Serine amide
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100
D-threonine amide
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-
0.25
Gly 4-nitroanilide
pH 9.0, 30°C
22.3
glycine amide
-
-
6.7
L-Ala 4-nitroanilide
pH 9.0, 30°C
49
Nalpha,Nalpha-Ac2-L-Lys-D-Ala-D-Ala
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mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
185
Nalpha-Ac-L-Lys-D-Ala-D-Ala
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mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
26 - 29
nitrocefin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2550
D-Ala 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
33 - 580
D-Ala-4-nitroanilide
2783
Gly 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
2100
L-Ala 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
0.62
Nalpha, Nalpha-Ac2-L-Lys-D-Ala-D-Ala
Ochrobactrum anthropi
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mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
0.2
Nalpha-Ac-L-Lys-D-Ala-D-Ala
Ochrobactrum anthropi
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mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
0.0008 - 0.0016
nitrocefin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7750
D-Ala 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
115522
11000
Gly 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
93512
313
L-Ala 4-nitroanilide
Aspergillus oryzae
G7H7Y1
pH 9.0, 30°C
49145
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
nitrocefin
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pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
pH 8.0, presence of ZnSO4
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
2% of maximum activity
7
20% of maximum activity
8
60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30184
8 * 31000, SDS-PAGE, 8 * 30184, calculated, 8 * 30909, mass spectrometry of His-tagged protein
30909
8 * 31000, SDS-PAGE, 8 * 30184, calculated, 8 * 30909, mass spectrometry of His-tagged protein
31000
8 * 31000, SDS-PAGE, 8 * 30184, calculated, 8 * 30909, mass spectrometry of His-tagged protein
57257
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x * 57257, calculation from nucleotide sequence
59000
-
2 * 59000, SDS-PAGE
59300
2 * 59300, calculated
122000
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gel filtration
126300
gel filtration
230000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 31000, SDS-PAGE, 8 * 30184, calculated, 8 * 30909, mass spectrometry of His-tagged protein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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30°C, 1 h, no loss of activity
647079
8 - 11
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731193
8
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45°C, 10 min, about 80% of the original activity retained
647079
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
pH 7.0-10.9, 1 h, no loss of activity
45
-
pH 8.0, 10 min, about 80% of original activity retained
60
10 min, stable
75
10 min, 20% residual activity
additional information
-
mutant enzymes with increased thermal stability
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression in Aspergillus oryzae
mutant enzymes with increased thermal stability
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme consists of N-terminal domain DAP-A and C-terminal domains DAP-B and DAB-C. Coexpression of DAP-A plus DAP-BC results in a complex that copurifies on Ni-NTA-column and shows a 10fold increase in KM-value compared to wild-type. Mutant lacking gamma-loop residues 476-486, no enzymic activity but small D,D-carboxypeptidase and beta-lactamase activty. Mutant lacking gamma-loop residues 476-486 plus mutation N275R, no enzymic activity but small D,D-carboxypeptidase and beta-lactamase act
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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production of D-amino acids from L-amino acid amides by combination of alpha-amino-epsilon-caprolactam racemase, EC 5.1.1.15, and enzyme. Yield of conversion of L-alanine amid is more than 99%
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