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EC Tree
The taxonomic range for the selected organisms is: Escherichia coli 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, odc-paralogue, xodc2, adometdc/odc, ddodc,
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Decarboxylase, ornithine
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-
-
-
dODC
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degradative ornithine decarboxylase
ODC
-
-
-
-
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L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
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L-ornithine
putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
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L-ornithine
putrescine + CO2
-
-
-
?
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pyridoxal 5'-phosphate
-
cofactor
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antizyme
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non-competitive inhibitor protein isolated from Thermus thermophilus or Escherichia coli, almost complete inhibition at higer concentrations
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Ornithine decarboxylase antizyme
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purification of the protein inhibitor
-
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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
3.6
L-Orn
-
degradative ornithine decarboxylase
5.6
L-Orn
-
biosynthetic ornithine decarboxylase
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additional information
additional information
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-
-
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
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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
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130
-
degradative ornithine decarboxylase
99
-
biosynthetic ornithine decarboxylase
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6.9
-
degradative ornithine decarboxylase
8.3
-
biosynthetic ornithine decarboxylase
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-
UniProt
brenda
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80000
-
2 * 80000, degradative ornithine decarboxylase
81000
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2 * 81000, biosynthetic ornithine decarboxylase
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dimer
-
2 * 81000, biosynthetic ornithine decarboxylase
dimer
-
2 * 80000, degradative ornithine decarboxylase
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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
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E165A
1.9fold increase in catalytic efficiency
E165G
1.8fold increase in catalytic efficiency
E165S
5.1fold increase in catalytic efficiency
E165T
36fold increase in catalytic efficiency
E165V
7.4fold increase in catalytic efficiency
I163A
2.4fold increase in catalytic efficiency
I163G
2.4fold increase in catalytic efficiency
I163S
4.7fold increase in catalytic efficiency
I163T
17.6fold increase in catalytic efficiency
I163T/E165T
62.5fold increase in catalytic efficiency
I163V
3.4fold increase in catalytic efficiency
I163V/E165V
22.7fold increase in catalytic efficiency
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a biosynthetic ornithine decarboxylase and a degradative ornithine decarboxylase
-
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Kyriakidis, D.A.; Heller, J.S.; Canellakis, E.S.
Purification of ornithine decarboxylase antizymes (Escherichia coli)
Methods Enzymol.
94
193-199
1983
Escherichia coli
brenda
Morris, D.R.; Boeker, E.A.
Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli
Methods Enzymol.
94
125-134
1983
Escherichia coli
brenda
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
brenda
Choi, H.; Kyeong, H.; Choi, J.; Kim, H.
Rational design of ornithine decarboxylase with high catalytic activity for the production of putrescine
Appl. Microbiol. Biotechnol.
98
7483-7490
2014
Escherichia coli (P21169), Escherichia coli
brenda