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Information on EC 3.4.11.19 - D-stereospecific aminopeptidase
for references in articles please use BRENDA:EC3.4.11.19
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.11 Aminopeptidases
3.4.11.19 D-stereospecific aminopeptidase
IUBMB Comments
Known from the bacterium Ochrobactrum anthropi. In peptidase family S12 (D-Ala-D-Ala carboxypeptidase family)
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 3.4.11.19
- ochrobactrum
- anthropi
- beta-lactamases
-
penicillin-binding
-
penicillin-recognizing
- aminopeptidases
-
point-group
- d,d-carboxypeptidase
-
non-sporulating
- synthesis
Reaction Schemes
showRelease 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
Synonyms
d-aminopeptidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-aminopeptidase
DAP
D-aminopeptidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
57534-78-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-2-aminobutanamide + H2O
D-aminobutanoic acid + NH3
-
Substrates: racemic, preferred substrate
Products: -
Products: -
?
D-alanine amide + H2O
D-alanine + NH3
-
Substrates: 28.3% of the activity with D-2-aminobutanamide
Products: -
Products: -
?
D-alanine benzylamide + H2O
D-Ala + benzylamine
-
Substrates: -
Products: -
Products: -
?
D-alanine n-butylamide + H2O
D-Ala + n-butylamine
-
Substrates: -
Products: -
Products: -
?
fluoresceyl-Gly-6-aminopenicillanic acid + H2O
?
-
Substrates: penicillin-binding activity of mutant lacking residues 476-486
Products: -
Products: -
?
glycine amide + H2O
glycine + NH3
-
Substrates: 29.6% of the activity with D-2-aminobutanamide
Products: -
Products: -
?
L-2-aminobutyric amide + H2O
D-2-aminobutyric acid + NH3
-
Substrates: in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Products: -
Products: -
?
L-alanine amide + H2O
D-alanine + NH3
-
Substrates: in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Products: -
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?
L-methionine amide + H2O
D-methionine + NH3
-
Substrates: in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Products: -
Products: -
?
L-serine amide + H2O
D-serine + NH3
-
Substrates: in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Products: -
Products: -
?
Nalpha, Nalpha-Ac2-L-Lys-D-Ala-D-Ala + H2O
Nalpha, Nalpha-Ac2-L-Lys-D-Ala + D-Ala
-
Substrates: wild-type, no substrate. Mutant lacking residues 476-486 with or without mutation N275R, small D,D-carboxypeptidase activity
Products: -
Products: -
?
Nalpha-Ac-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Ac-L-Lys-D-Ala + D-Ala
-
Substrates: wild-type and mutant lacking residues 476-486, no substrate. Mutant lacking residues 476-486 plus mutation N275R, small D,D-carboxypeptidase activity
Products: -
Products: -
?
(R)-2-aminobutanamide + H2O
(R)-2-aminobutanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(R)-2-aminobutanamide + H2O
(R)-2-aminobutanoic acid + NH3
Brucella anthropi C1-38
-
Substrates: -
Products: -
Products: -
?
D-2-aminobutyric acid amide + H2O
D-aminobutyric acid + NH3
-
Substrates: -
Products: -
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?
D-2-aminobutyric acid amide + H2O
D-aminobutyric acid + NH3
Brucella anthropi SCRC C1-38
-
Substrates: -
Products: -
Products: -
?
D-Ala 4-nitroanilide + H2O
D-Ala + 4-nitroaniline
Substrates: 93% of the activity with Gly 4-nitroanilide
Products: -
Products: -
?
D-Ala 4-nitroanilide + H2O
D-Ala + 4-nitroaniline
-
Substrates: 93% of the activity with Gly 4-nitroanilide
Products: -
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?
D-Ala 4-nitroanilide + H2O
D-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Ala 4-nitroanilide + H2O
D-Ala + 4-nitroaniline
Brucella anthropi SCRC C1-38
-
Substrates: -
Products: -
Products: -
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Ala 4-nitroanilide + H2O
L-Ala + 4-nitroaniline
Substrates: 12% of the activity with Gly 4-nitroanilide
Products: -
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?
L-Ala 4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
Substrates: 12% of the activity with Gly 4-nitroanilide
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows strict D-stereospecific aminopeptidase activity. No or very poor activity with beta-Ala 4-nitroanilide, L-Leu 4-nitroanilide, D-Leu 4-nitroanilide,L-Met 4-nitroanilide, L-Pro 4-nitroanilide, L-Val 4-nitroanilide, L-Ile 4-nitroanilide, L-Phe 4-nitroanilide, D-Phe 4-nitroanilide, L-Lys 4-nitroanilide, L-Arg 4-nitroanilide, L-His 4-nitroanilide, L-Asp 4-nitroanilide, L-Glu 4-nitroanilide. No substrates: L-Ala-Gly and L-Cys-Gly dipeptides and L-Cys-Gly-Gly tripeptide
Products: -
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?
additional information
?
-
-
Substrates: enzyme shows strict D-stereospecific aminopeptidase activity. No or very poor activity with beta-Ala 4-nitroanilide, L-Leu 4-nitroanilide, D-Leu 4-nitroanilide,L-Met 4-nitroanilide, L-Pro 4-nitroanilide, L-Val 4-nitroanilide, L-Ile 4-nitroanilide, L-Phe 4-nitroanilide, D-Phe 4-nitroanilide, L-Lys 4-nitroanilide, L-Arg 4-nitroanilide, L-His 4-nitroanilide, L-Asp 4-nitroanilide, L-Glu 4-nitroanilide. No substrates: L-Ala-Gly and L-Cys-Gly dipeptides and L-Cys-Gly-Gly tripeptide
Products: -
Products: -
?
additional information
?
-
Substrates: substrates beta-Ala-4-nitroanilide, L-Leu-4-nitroanilide, D-Leu-4-nitroanilide, L-Met-4-nitroanilide, L-Pro-4-nitroanilide, L-Val-4-nitroanilide, L-Ile-4-nitroanilide, L-Phe-4-nitroanilide, D-Phe-4-nitroanilide, L-Lys-4-nitroanilide, L-Arg-4-nitroanilide, L-His-4-nitroanilide, L-Asp-4-nitroanilide, L-Glu-4-nitroanilide show less than 0.5% of the activity with Gly-4-nitroanilide, no substrates: L-Ala-Gly and L-Cys-Gly dipeptides and L-Cys-Gly-Gly tripeptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates beta-Ala-4-nitroanilide, L-Leu-4-nitroanilide, D-Leu-4-nitroanilide, L-Met-4-nitroanilide, L-Pro-4-nitroanilide, L-Val-4-nitroanilide, L-Ile-4-nitroanilide, L-Phe-4-nitroanilide, D-Phe-4-nitroanilide, L-Lys-4-nitroanilide, L-Arg-4-nitroanilide, L-His-4-nitroanilide, L-Asp-4-nitroanilide, L-Glu-4-nitroanilide show less than 0.5% of the activity with Gly-4-nitroanilide, no substrates: L-Ala-Gly and L-Cys-Gly dipeptides and L-Cys-Gly-Gly tripeptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: strict D-stereospecificity, the enzyme prefers peptides to amino acid arylamides or amino acid amides
Products: -
Products: -
?
additional information
?
-
Brucella anthropi SCRC C1-38
-
Substrates: strict D-stereospecificity, the enzyme prefers peptides to amino acid arylamides or amino acid amides
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-valine amide, D-proline amide and D-leucine amide show less than 2% of hte activity with D-2-aminobutanamide. No activity with D-arginine amide, D-phenylalanine amide, or with L-amino acid amides
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitrocefin
-
inhibitory on D,D-carboxypeptidase activity of mutant lacking residues 476-486 plus mutation N275R
additional information
-
probably has serine at the active centre, not: EDTA (0.2 mM)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
49
Nalpha,Nalpha-Ac2-L-Lys-D-Ala-D-Ala
-
mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
185
Nalpha-Ac-L-Lys-D-Ala-D-Ala
-
mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
0.51
D-Ala-4-nitroanilide
-
mutant lacking residues 476-486 plus domains DAP-BC, pH 8.0, 30°C
5.1
D-Ala-4-nitroanilide
-
complex of domain DAP-A plus domains DAP-BC, pH 8.0, 30°C
26
nitrocefin
-
mutant lacking residues 476-486 plus mutation N275R, pH 7.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.62
Nalpha, Nalpha-Ac2-L-Lys-D-Ala-D-Ala
-
mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
0.2
Nalpha-Ac-L-Lys-D-Ala-D-Ala
-
mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C
33
D-Ala-4-nitroanilide
-
mutant lacking residues 476-486 plus domains DAP-BC, pH 8.0, 30°C
210
D-Ala-4-nitroanilide
-
complex of domain DAP-A plus domains DAP-BC, pH 8.0, 30°C
0.0008
nitrocefin
-
mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
physiological function
GdaA is largely responsible for intracellular glycine and D-alanine aminopeptidase activities in Aspergillus oryzae during stationary-phase growth in liquid media. In addition, the activity increases in response to the depletion of nitrogen or carbon sources in the growth media. No significant differences are observed in the vegetative growth and conidiation on minimal and complete media in the GdaA deletion or overexpression strains, and control strains
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
126300
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
octamer
8 * 31000, SDS-PAGE, 8 * 30184, calculated, 8 * 30909, mass spectrometry of His-tagged protein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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 activity. Mutant lacking gamma-loop residues 476-486 plus mutation N275R, no enzymic activity but small D,D-carboxypeptidase and beta-lactamase activity.
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
-
at 50°C the rate of conversion is decreased because of the instability of DAP at higher temperatures
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, purified GdaA might be digested during the final step of purification without affecting the activity and dimerization under nondenaturing conditions