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Information on EC 3.5.1.16 - acetylornithine deacetylase and Organism(s) Escherichia coli and UniProt Accession P23908
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3.5.1.16 acetylornithine deacetylaseIUBMB Comments
Also hydrolyses N-acetylmethionine.
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Word Map
- 3.5.1.16
- argininosuccinase
-
argecbh
- p-beta-gal
-
desuccinylase
-
deacylase
- phospho-beta-glucosidase
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acetylornithine deacetylase, acetylornithinase, aoase, n-acetylornithine deacetylase, n-acetylornithinase, at4g17830, n-acetyl-l-ornithine deacetylase, arge-encoded n-acetyl-l-ornithine deacetylase, naogact, nao deacetylase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylornithinase
-
-
-
-
AO
-
-
-
-
N-acetylornithinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
N2-acetyl-L-ornithine amidohydrolase
Also hydrolyses N-acetylmethionine.
CAS REGISTRY NUMBER
COMMENTARY
9025-12-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2-acety-L-ornithine + H2O
L-ornithine + acetate
step in arginine biosynthesis
-
-
?
N2-acety-L-ornithine + H2O
L-ornithine + acetate
-
step in arginine biosynthesis
-
-
?
Nalpha-acetyl-L-ornithine + H2O
L-ornithine + acetate
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2-acety-L-ornithine + H2O
L-ornithine + acetate
step in arginine biosynthesis
-
-
?
N2-acety-L-ornithine + H2O
L-ornithine + acetate
-
step in arginine biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Co2+
Zn2+
additional information
-
90% of full activity upon addition of one metal ion
Zn2+
-
0.1 mM activity increases 2-fold, further increase in concentration results in inhibition
Zn2+
-
required, the enzyme binds two Zn(II) ions in non-interactive binding sites with Kd values for the first Zn(II) binding event of 0.0027 mM, whereas the observed Kd values for the second metal binding event in DapE is 0.051 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-6-[(4-carboxy-3,3-dimethylbutanoyl)amino]heptanedioic acid
-
slight inhibition
2-amino-6-[(4-carboxy-3-methylbutanoyl)amino]heptanedioic acid
-
slight inhibition
2-amino-6-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]heptanedioic acid
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slight inhibition
[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]leucine
-
bestatin, competitive inhibitor
additional information
-
mono-N-acyl derivatives of 2,6-diaminopimelic acid as enzyme inhibitors, overview. No inhibition by 2-amino-6-[(2-methylpropanoyl)amino]heptanedioic acid, 2-amino-6-(butanoylamino)heptanedioic acid, 2-amino-6-[(2,2-dimethylpropanoyl)amino]heptanedioic acid, 2-amino-6-(pentanoylamino)heptanedioic acid, 2-amino-6-(benzoylamino)heptanedioic acid, 2-amino-6-[(4-carboxybutanoyl)amino]heptanedioic acid, 2-amino-6-[(4-carboxy-2,2,3,3-tetrafluorobutanoyl)amino]heptanedioic acid, 2-amino-6-[(3-ethoxy-3-oxopropanoyl)amino]heptanedioic acid, and 2-amino-6-[[(2R)-4-methoxy-2-methylpent-4-enoyl]amino]heptanedioic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
N-acetyl-L-ornithine
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in the presence of one equivalent of Zn(II), pH 7.5, 25°C
1.2
N-acetyl-L-ornithine
-
in the presence of one equivalent of Co(II), pH 7.5, 25°C
0.8
N-alpha-acetyl-L-ornithine
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in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Mn2+ or Zn2+
1.2
N-alpha-acetyl-L-ornithine
-
in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Co2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1600
N-acetyl-L-ornithine
-
in the presence of one equivalent of Zn(II), pH 7.5, 25°C
3800
N-acetyl-L-ornithine
-
in the presence of one equivalent of Co(II), pH 7.5, 25°C
550
N-alpha-acetyl-L-ornithine
-
in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Mn2+
1600
N-alpha-acetyl-L-ornithine
-
in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Zn2+
3800
N-alpha-acetyl-L-ornithine
-
in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Co2+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.11
2-amino-6-[(4-carboxy-3,3-dimethylbutanoyl)amino]heptanedioic acid
Escherichia coli
-
pH 7.5, 25°C
1.28
2-amino-6-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]heptanedioic acid
Escherichia coli
-
pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
three-dimensional homologic structure, molecular modeling using the X-ray crystal structure of the DapE from Haemophilus influenzae, PDB ID 3IC1, as template, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42320
calculated polypeptide, corresponding to AO nucleotide sequence
42000
42350
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H355A
-
site-directed mutagenesis, the mutation affects a key aspect of the active site of the enzyme, i.e. metal cofactor binding. The mutant contains no Zn2+ ions but requires Zn2+ for activity, decrease in activity of H355A due to a 380fold decrease in kcat. The catalytic efficiency for the Co(II)-loaded H355A mutant enzyme is about 160fold less than the Co(II)-loaded wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli transformed with pTrc99A + pC-28 containing argE, lambdaZAP library from 2674
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gene argE, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21, wild-type and mutant H355A are soluble, the other mutants are insoluble
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding of mutants H355K, H80A, and H80K from inclusion bodies after recombinant expression in Escherichia coli strain BL21 is not sucessfull
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vogel, H.J.; Bonner, D.M.
Acetylornithinase of Escherichia coli: Partial purification and some properties
J. Biol. Chem.
218
97-106
1956
Aerobacter sp., Erwinia sp., Escherichia coli, Escherichia coli 160-37, Escherichia coli ATCC 9637, Escherichia coli B / ATCC 11303, Klebsiella sp., Proteus sp., Salmonella sp., Serratia sp., Shigella sp.
Boyen, A.; Charlier, D.; Charlier, J.; Sakanyan, V.; Mett, I.; Glansdorff, N.
Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related
Gene
116
1-6
1992
Escherichia coli (P23908), Escherichia coli
Meinnel, T.; Schmitt, E.; Mechulam, Y.; Blanquet, S.
Structural and biochemical characterization of the Escherichia coli arg gene product
J. Bacteriol.
174
2323-2331
1992
Escherichia coli, Escherichia coli 160-37, Escherichia coli ATCC 9637, Saccharomyces sp.
Xu, Y.; Liang, Z.; Legrain, C.; Rueger, H.J.; Glansdorff, N.
Evolution of arginine biosynthesis in the bacterial domain: Novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase
J. Bacteriol.
182
1609-1615
2000
Escherichia coli, Escherichia coli 160-37, Escherichia coli ATCC 9637, Moritella abyssi, Moritella profunda
Javid-Majd, F.; Blanchard, J.S.
Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase
Biochemistry
39
1285-1293
2000
Escherichia coli, Escherichia coli 160-37, Escherichia coli ATCC 9637
McGregor, W.C.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli contains a dinuclear metalloactive site
J. Am. Chem. Soc.
127
14100-14107
2005
Escherichia coli, Escherichia coli BL21 (DE3)
McGregor, W.C.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
Characterization of the catalytically active Mn(II)-loaded argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli
J. Biol. Inorg. Chem.
12
603-613
2007
Escherichia coli
Tao, Y.; Shokes, J.; McGregor, W.; Scott, R.; Holz, R.
Structural characterization of Zn(II)-, Co(II)-, and Mn(II)-loaded forms of the argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli
J. Inorg. Biochem.
111
157-163
2012
Escherichia coli
Hlavacek, J.; Vitovcova, M.; Sazelova, P.; Picha, J.; Vanek, V.; Budesinsky, M.; Jiracek, J.; Gillner, D.M.; Holz, R.C.; Miksik, I.; Kasicka, V.
Mono-N-acyl-2,6-diaminopimelic acid derivatives: analysis by electromigration and spectroscopic methods and examination of enzyme inhibitory activity
Anal. Biochem.
467
4-13
2014
Escherichia coli
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