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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Escherichia coli and UniProt Accession P21169
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4.1.1.17 ornithine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
-
n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
-
antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
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
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, xodc2, adometdc/odc, ddodc, odc-paralogue, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bODC
-
-
-
-
Decarboxylase, ornithine
-
-
-
-
ODC
ODC-paralogue
-
-
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
ODC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
-
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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antizyme
-
non-competitive inhibitor protein isolated from Thermus thermophilus or Escherichia coli, almost complete inhibition at higer concentrations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
L-ornithine
mutant I163T, pH 7.0, temperature not specified in the publication
0.6
L-ornithine
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
0.7
L-ornithine
mutant E165T, pH 7.0, temperature not specified in the publication
1.1
L-ornithine
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
1.3
L-ornithine
mutant I163V, pH 7.0, temperature not specified in the publication
1.4
L-ornithine
mutant E165V, pH 7.0, temperature not specified in the publication
1.5
L-ornithine
mutant I163A, pH 7.0, temperature not specified in the publication
1.5
L-ornithine
mutant I163S, pH 7.0, temperature not specified in the publication
1.7
L-ornithine
mutant I163G, pH 7.0, temperature not specified in the publication
1.9
L-ornithine
mutant E165S, pH 7.0, temperature not specified in the publication
2.4
L-ornithine
mutant E165A, pH 7.0, temperature not specified in the publication
3
L-ornithine
mutant E165G, pH 7.0, temperature not specified in the publication
3.3
L-ornithine
wild-type, pH 7.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
L-ornithine
wild-type, pH 7.0, temperature not specified in the publication
3.6
L-ornithine
mutant I163A, pH 7.0, temperature not specified in the publication
4.2
L-ornithine
mutant I163G, pH 7.0, temperature not specified in the publication
4.4
L-ornithine
mutant I163V, pH 7.0, temperature not specified in the publication
4.8
L-ornithine
mutant E165A, pH 7.0, temperature not specified in the publication
5.6
L-ornithine
mutant E165G, pH 7.0, temperature not specified in the publication
7.4
L-ornithine
mutant I163S, pH 7.0, temperature not specified in the publication
10.1
L-ornithine
mutant E165S, pH 7.0, temperature not specified in the publication
10.1
L-ornithine
mutant I163T, pH 7.0, temperature not specified in the publication
10.9
L-ornithine
mutant E165V, pH 7.0, temperature not specified in the publication
24.8
L-ornithine
mutant E165T, pH 7.0, temperature not specified in the publication
25.7
L-ornithine
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
38.5
L-ornithine
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
L-ornithine
wild-type, pH 7.0, temperature not specified in the publication
1.8
L-ornithine
mutant I163T, pH 7.0, temperature not specified in the publication
1.9
L-ornithine
mutant E165G, pH 7.0, temperature not specified in the publication
2
L-ornithine
mutant E165A, pH 7.0, temperature not specified in the publication
2.3
L-ornithine
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
2.4
L-ornithine
mutant I163A, pH 7.0, temperature not specified in the publication
2.5
L-ornithine
mutant I163G, pH 7.0, temperature not specified in the publication
3.5
L-ornithine
mutant I163V, pH 7.0, temperature not specified in the publication
3.7
L-ornithine
mutant E165T, pH 7.0, temperature not specified in the publication
4.8
L-ornithine
mutant I163S, pH 7.0, temperature not specified in the publication
5.2
L-ornithine
mutant E165S, pH 7.0, temperature not specified in the publication
6.4
L-ornithine
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
7.6
L-ornithine
mutant E165V, pH 7.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on the crystal structure of ODC from Lactobacillus 30a, PDB entry 1ORD. The model reveals an unusually deep and narrow shape of the substrate tunnel. Amino acids at the substrate entry site are V156, D160, I163, E165, E689, and Q691
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a biosynthetic ornithine decarboxylase and a degradative ornithine decarboxylase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kyriakidis, D.A.; Heller, J.S.; Canellakis, E.S.
Purification of ornithine decarboxylase antizymes (Escherichia coli)
Methods Enzymol.
94
193-199
1983
Escherichia coli
Morris, D.R.; Boeker, E.A.
Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli
Methods Enzymol.
94
125-134
1983
Escherichia coli
Pantazaki, A.A.; Anagnostopoulos, C.G.; Lioliou, E.E.; Kyriakidis, D.A.
Characterization of ornithine decarboxylase and regulation by its antizyme in Thermus thermophilus
Mol. Cell. Biochem.
195
55-64
1999
Escherichia coli, Thermus thermophilus
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