Information on EC 3.5.1.16 - acetylornithine deacetylase

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

EC NUMBER
COMMENTARY hide
3.5.1.16
-
RECOMMENDED NAME
GeneOntology No.
acetylornithine deacetylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-acetyl-L-ornithine + H2O = acetate + L-ornithine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-arginine biosynthesis III (via N-acetyl-L-citrulline)
-
-
L-ornithine biosynthesis I
-
-
Metabolic pathways
-
-
arginine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
N2-acetyl-L-ornithine amidohydrolase
Also hydrolyses N-acetylmethionine.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-12-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aerobacter sp.
-
-
-
Manually annotated by BRENDA team
gene atnaod or At4g17830
UniProt
Manually annotated by BRENDA team
gene atnaod or At4g17830
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BL21 (DE3)
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
psychrophilic Vibrionaceae
-
-
Manually annotated by BRENDA team
psychrophilic Vibrionaceae
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-DL-methionine + H2O
methionine + acetate
show the reaction diagram
N-acetyl-L-ornithine + H2O
acetate + L-ornithine
show the reaction diagram
-
-
-
-
?
N-acetylformylmethionine + H2O
?
show the reaction diagram
N-alpha-acetyl-L-ornithine + H2O
?
show the reaction diagram
-
-
-
-
?
N2-acety-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
N2-acetyl-L-ornithine + H2O
acetate + L-ornithine
show the reaction diagram
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
Nalpha-acetyl-DL-serine + H2O
DL-serine + acetate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
Nalpha-acetyl-L-asparagine + H2O
L-asparagine + acetate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-cysteine + H2O
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
Nalpha-acetyl-L-leucine + H2O
L-leucine + acetate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-lysine + H2O
L-lysine + acetate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
Nalpha-benzoyl-L-ornithine + H2O
benzoate + ornithine
show the reaction diagram
Nalpha-chloroacetylglycine + H2O
glycine + chloroacetate
show the reaction diagram
-
-
-
-
?
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
N2-acety-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
N2-acetyl-L-ornithine + H2O
acetate + L-ornithine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PO43-
-
activation
additional information
-
90% of full activity upon addition of one metal ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
zinc-specific chelator
2-(acetylamino)-6-aminoheptanedioic acid
-
-
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-[(4-carboxybutanoyl)amino]heptanedioic acid
-
-
2-amino-6-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]heptanedioic acid
-
slight inhibition
3-(ethylamino)piperidin-2-one
-
-
acetate
-
product inhibition
N2-(2,2-dimethylpropanoyl)-L-ornithine
-
-
N2-(2-methylpropanoyl)-L-ornithine
-
-
N2-(ethoxycarbonyl)-L-ornithine
-
weak inhibition
N2-(methoxycarbonyl)-L-ornithine
-
-
N2-(propoxycarbonyl)-L-ornithine
-
-
N2-(tert-butoxycarbonyl)-L-ornithine
-
-
N2-(trifluoroacetyl)-L-ornithine
-
weak inhibition
N2-acetyl-D-ornithine
-
weak inhibition
N2-butanoyl-L-ornithine
-
-
N2-chloroacetyl-L-ornithine
-
-
N2-dichloroacetyl-L-ornithine
-
-
N2-ethyl-L-ornithine
-
-
N2-propanoyl-L-ornithine
-
-
N2-trichloroacetyl-D-ornithine
-
-
N2-trichloroacetyl-L-ornithine
-
-
N2-[(propan-2-yloxy)carbonyl]-L-ornithine
-
-
N2-[[(2-methylpentan-2-yl)oxy]carbonyl]-L-ornithine
-
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NaF
-
linear uncompetitive inhibition
ornithine
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product inhibition
p-chloromercuribenzoate
-
-
[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]leucine
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bestatin, competitive inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
-
-
phosphate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.56 - 2.2
acetylornithine
0.8 - 1.2
N-acetyl-L-ornithine
0.8 - 1.2
N-alpha-acetyl-L-ornithine
0.8 - 1.2
N2-Acetyl-L-ornithine
6.7
Nalpha-acetyl-DL-serine
-
-
1
Nalpha-acetyl-L-alanine
-
-
8.3
Nalpha-acetyl-L-asparagine
-
-
13
Nalpha-acetyl-L-cysteine
-
-
2.4
Nalpha-acetyl-L-glutamine
-
-
7
Nalpha-acetyl-L-leucine
-
-
4.1
Nalpha-acetyl-L-lysine
-
-
0.81
Nalpha-acetyl-L-methionine
-
-
1.3 - 7.2
Nalpha-Acetyl-L-ornithine
2
Nalpha-acetylformyl-L-methionine
-
-
7
Nalpha-chloroacetylglycine
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1600 - 3800
N-acetyl-L-ornithine
550 - 3800
N-alpha-acetyl-L-ornithine
1600 - 3800
N2-Acetyl-L-ornithine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]leucine
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
2-(acetylamino)-6-aminoheptanedioic acid
Escherichia coli
-
pH 7.5, 25°C
2.11
2-amino-6-[(4-carboxy-3,3-dimethylbutanoyl)amino]heptanedioic acid
Escherichia coli
-
pH 7.5, 25°C
2.63
2-amino-6-[(4-carboxybutanoyl)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
2.5
3-(ethylamino)piperidin-2-one
Bacillus subtilis
-
pH 7.5, 25°C
5.4
N2-(2,2-dimethylpropanoyl)-L-ornithine
Bacillus subtilis
-
about, pH 7.5, 25°C
1.21
N2-(2-methylpropanoyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.25
N2-(ethoxycarbonyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
1.01
N2-(methoxycarbonyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.71
N2-(propoxycarbonyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.54
N2-(tert-butoxycarbonyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.2
N2-(trifluoroacetyl)-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.41
N2-acetyl-D-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.42
N2-butanoyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.085
N2-chloroacetyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.34
N2-dichloroacetyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
2.7
N2-ethyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.76
N2-propanoyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.32
N2-trichloroacetyl-D-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
0.45
N2-trichloroacetyl-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
1.4
N2-[(propan-2-yloxy)carbonyl]-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
1.16
N2-[[(2-methylpentan-2-yl)oxy]carbonyl]-L-ornithine
Bacillus subtilis
-
pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
-
pH 8.0, 70°C, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
0.15
-
pH 8.0, 70°C, activity in cell culture in growth medium with 0.2% yeast extract
2000
-
2 mM N2-acetyl-L-ornithine at 25 °C and pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 8.7
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest enzyme level in unfertilized ovules
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Xanthomonas campestris pv. campestris (strain 8004)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42320
calculated polypeptide, corresponding to AO nucleotide sequence
52000
-
SDS-PAGE
62000
-
gel filtration
77000
-
nondenaturing PAGE
100000
native enzyme, gel filtration
170000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 42350, calculated, corresponds to SDS-PAGE analysis
octamer
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 55
-
-
20 - 45
-
50 mM Chelex 100 treated phosphate buffer at pH 7.5
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fast-flow Q-Sepharose column chromatography
-
purification of recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
argE gene encoding enzyme cloned and sequenced, M13
Escherichia coli transformed with pTrc99A + pC-28 containing argE, lambdaZAP library from 2674
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
-
gene At4g17830, located on chromosome IV and organized into nine exons, which encodes two putative isozymes, UniProt IDs F4JPZ7 and Q9C5C4, sequence comparison and phylogenetic analysis
PCR-amplified argE, cloned and expressed
-
plasmid pMC7
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no repression by arginine
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
H355K
-
site-directed mutagenesis
H80A
-
site-directed mutagenesis
H80K
-
site-directed mutagenesis
additional information
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 hide
LITERATURE
medicine
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