Ligand L-ornithine

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Basic Ligand Information

Molecular Structure
Picture of L-ornithine (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C5H12N2O2
L-ornithine
AHLPHDHHMVZTML-BYPYZUCNSA-N
Synonyms:
5-amino-L-norvaline, alpha-ornithine, L-2,5-diaminopentanoate, L-alpha-Orn, L-Orn, L-ornithine[side 2], Orn, ornithine
Pathway Source
Pathways


Show all pahtways known for Show all BRENDA pathways known for L-ornithine

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (36 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O
-
show the reaction diagram
L-ornithine + O2 + H2O = 5-amino-2-oxopentanoate + NH3 + H2O2
-
show the reaction diagram
L-ornithine + O2 + H2O = (2S)-2-hydroxy-5-oxopentanoate + NH3 + H2O2
-
show the reaction diagram
L-ornithine + 2-oxoglutarate + NADPH = N2-(1,3-dicarboxypropyl)-L-ornithine + NADP+ + H2O
-
show the reaction diagram
carbamoyl phosphate + L-ornithine = phosphate + N-carbamoyl-L-ornithine
-
show the reaction diagram
L-ornithine + guanidinoacetate = L-arginine + glycine
show the reaction diagram
L-ornithine + L-homoarginine = L-arginine + L-lysine
-
show the reaction diagram
succinyl-CoA + L-ornithine = CoA + N2-succinyl-L-ornithine
-
show the reaction diagram
benzoyl-CoA + L-ornithine = CoA + N2,N5-dibenzoyl-L-ornithine
-
show the reaction diagram
acetyl phosphate + L-ornithine = phosphate + N5-acetyl-L-ornithine
-
show the reaction diagram
L-ornithine + a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a lyso-ornithine lipid + a holo-[acyl-carrier protein]
-
show the reaction diagram
L-2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + L-glutamate
-
show the reaction diagram
L-ornithine = putrescine + CO2
-
show the reaction diagram
L-ornithine = putrescine + CO2
-
show the reaction diagram
L-Ornithine = D-Ornithine
-

In Vivo Product in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
N2-(D-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH
-
-
show the reaction diagram
L-arginine + glycine = L-ornithine + guanidinoacetate
-
show the reaction diagram
L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate = L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate
-
-
show the reaction diagram
L-arginine + L-lysine = L-ornithine + L-homoarginine
-
-
show the reaction diagram
N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
-
show the reaction diagram
L-citrulline + H2O = L-ornithine + CO2 + NH3
-
-
show the reaction diagram
Nomega-hydroxy-L-arginine + H2O = L-ornithine + hydroxyurea
-

Substrate in Enzyme-catalyzed Reactions (125 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
L-ornithine + H2O + NAD+ = ? + NH3 + NADH
-
show the reaction diagram
L-ornithine + O2 + H2O = ?
-
show the reaction diagram
ornithine + H2O + O2 = ?
-
show the reaction diagram
L-ornithine + H2O + O2 = 2-oxoornithine + NH3 + H2O2
-
show the reaction diagram
L-ornithine + H2O + 2 cytochrome b = 2-oxo-5-aminopentanoate + NH3 + 2 reduced cytochrome b
-
show the reaction diagram
L-ornithine + 2-oxoglutarate + NADPH = N2-(1,3-dicarboxypropyl)-L-ornithine + NADP+ + H2O
-
show the reaction diagram
succinyl-CoA + L-ornithine = CoA + N2-succinyl-L-ornithine
-
show the reaction diagram
benzoyl-CoA + L-ornithine = CoA + N2,N5-dibenzoyl-L-ornithine
-
show the reaction diagram
acetyl phosphate + L-ornithine = phosphate + N5-acetyl-L-ornithine
-
show the reaction diagram
L-ornithine + N-acetyl-L-glutamate = N2-acetyl-L-ornithine + L-glutamate
show the reaction diagram
ornithine + casein = ?
-
show the reaction diagram
pyruvate + L-ornithine = L-alanine + ?
-
show the reaction diagram
L-ornithine + 2-oxoglutarate = L-glutamate + (S)-2-amino-5-oxopentanoate
-
show the reaction diagram
L-ornithine + 4,5-dioxopentanoate = 5-aminolevulinate + 5-amino-2-oxopentanoate
-
show the reaction diagram
L-2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + L-glutamate
-
show the reaction diagram
L-ornithine + 2-oxoglutarate = L-glutamate 5-semialdehyde + L-glutamate
-
show the reaction diagram
L-ornithine + 2-oxoglutarate = ?
-
show the reaction diagram
L-ornithine + H2O = ?
-
show the reaction diagram
L-ornithine = 1,4-diaminobutane + CO2
-
show the reaction diagram
L-ornithine = ?
-
show the reaction diagram
L-ornithine = ?
-
show the reaction diagram
L-ornithine = putrescine + CO2
-
show the reaction diagram
L-ornithine = ?
-
show the reaction diagram
L-Ornithine = D-Ornithine
-
show the reaction diagram
L-Ornithine = D-Ornithine
-
show the reaction diagram
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-ornithine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-ornithine
-
show the reaction diagram
ATP + gamma-L-Glu-L-Cys + L-Orn = ADP + phosphate + gamma-Glu-L-Cys-L-Orn
-
show the reaction diagram
ATP + H2O + L-Orn/out = ADP + phosphate + L-Orn/in
-

Product in Enzyme-catalyzed Reactions (92 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
alpha-N-(5'-phospho-4'-pyridoxyl)-ornithine + O2 + H2O = pyridoxal 5'-phosphate + alpha-ornithine + H2O2
-
show the reaction diagram
N2-(D-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH
-
-
show the reaction diagram
L-arginine + L-lysine = L-ornithine + L-homoarginine
-
-
show the reaction diagram
Orn-7-amido-4-methylcoumarin + H2O = Orn + 7-amino-4-methylcoumarin
-
show the reaction diagram
aminoacyl-L-ornithine + H2O = L-ornithine + acylamine
-
-
show the reaction diagram
hippuryl-L-Orn + H2O = hippuric acid + Orn
-
show the reaction diagram
L-Orn-L-Leu-D-Phe-L-Pro-L-Val-OH + H2O = L-Orn + L-Val + L-Leu-D-Phe-L-Pro-OH
-
-
show the reaction diagram
N-acetyl-L-ornithine + H2O = acetate + L-ornithine
-
-
show the reaction diagram
N-carbamoyl-L-ornithine + H2O = L-ornithine + CO2 + NH3
-
-
show the reaction diagram
N2-acetyl-L-ornithine + H2O = L-ornithine + acetate
-
-
show the reaction diagram
L-arginine + H2O = L-ornithine + urea
-
-
show the reaction diagram
Nomega-hydroxy-L-arginine + H2O = L-ornithine + hydroxyurea
-
-
show the reaction diagram
L-arginine + H2O = L-ornithine + urea
-
-
show the reaction diagram
D-ornithine = L-ornithine
-
-
show the reaction diagram
D-ornithine = L-ornithine
-
-
show the reaction diagram
D-ornithine = L-ornithine
-

Activator in Enzyme-catalyzed Reactions (106 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (119 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
at low concentration of L-lysine reaction is stimulated by L-ornithine, at high concentrations of L-lysine it is inhibited
-
inhibits only the short enzyme form
-
inhibition 10% by 10 mM L-ornithine
-
83% activity in the presence of 10 mM L-ornithine
-
pH 7.6, 30°C
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
-
3 mM, 39% loss of activity
-
complete inhibition of saccharopine formation, competitive with lysine
-
above 10 mM
-
above 8 mM
-
at high concentrations
-
at high concentrations; noncompetitive substrate inhibition vs. carbamoylphosphate
-
competitive vs. carbamoylphosphate in the presence of phosphate
-
recombinant wild-type enzyme
-
above 1 mg per ml guanidinoacetate-ornithine transamidination is inhibited
competitive inhibition
partial mixed product inhibition, L-ornithine therefore binds to the active site of CyrA at a binding site distinct from the hydroxylamine-binding site
product inhibition, most potent competitive inhibitor
-
feedback repression of L-ornithine synthesis, inhibition of OATase activity
product inhibition
weak, suicide substrate in the presence of casein
-
10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM
-
at high concentrations
-
concentration above 40 mM, slight inhibition
-
slight inhibition above 40 mM
-
substrate inhibition
-
competitive inhibitor of pyruvate-dependent GABA-T activity
-
moderate inhibitor; moderate inhibitor
-
20% inhibition
-
mixed inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
-
40% inhibition at 2 mM
-
43–65% inhibition at 1 mM
-
10 mM, 64% inhibition
-
higher inhibitory effect than with D-ornithine
-
12 mM, 10% inhibition
-
27% inhibition at 2 mM
31% enzyme inhibition at 2 mM
weak
-
caseinolytic activity
-
weak
-
product inhibition
-
competitive inhibitor
mixed type inhibition; mixed type inhibition
moderately inhibitory
product inhibition
noncompetitive inhibitor
10 mM, 12% loss of activity. 200 mM, 24% loss of activity
-
noncompetitive
-
0.001 mM in 0.2 mM Tris-HCl buffer
-
inhibition of Lys decarboxylation
-
L-Orn
-
competitive
-
inactivated by preliminary incubation at pH 10.0. The inactivation is prevented and the inactivated enzyme is reactivated by addition of pyruvate or oxaloacetate
-
poor inhibitor
-
competitive versus L-lysine
-

3D Structure of Enzyme-Ligand-Complex (PDB) (239 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (122 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.88
-
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
0.53
-
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
1.06
-
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.5
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.15
-
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
0.11
-
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.59
-
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
0.62
-
pH 8.0, 25°C
0.327
-
pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine
0.5
-
pH 7.5, 25°C, cosubstrate: NADH, oxygen consumption assay
0.68
-
pH 7.5, 25°C, cosubstrate: NADPH, following the formation of hydroxylated ornithine
0.48
-
pH 7.5, 25°C, cosubstrate: NADPH, oxygen consumption assay
0.87
-
pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH
0.03
-
pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH
0.03
-
recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication
0.2
-
recombinant holo-enzyme, pH 7.5, temperature not specified in the publication
0.34
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.0198
-
at pH 8.5 and 30°C
0.1
-
A240D/E277G double mutant, at 30°C
2900
-
A240D/E277G double mutant, at 55°C
4300
-
at 30°C
370
-
at 55°C
500
-
mutant enzyme C273A, at pH 8.5 and 20°C
170
-
mutant enzyme D140N, at pH 8.5 and 20°C
460
-
mutant enzyme D231A, at pH 8.5 and 20°C
0.7
-
mutant enzyme E299D, at pH 8.5 and 20°C
170
-
mutant enzyme E299Q, at pH 8.5 and 20°C
5.1
-
mutant enzyme H272L, at pH 8.5 and 20°C
4.3
-
mutant enzyme H272N, at pH 8.5 and 20°C
95
-
mutant enzyme Q104L, at pH 8.5 and 20°C
52
-
mutant enzyme R57A, at pH 8.5 and 20°C
8.2
-
mutant enzyme S61A, at pH 8.5 and 20°C
240
-
mutant enzyme Y160F, at pH 8.5 and 20°C
110
-
mutant enzyme Y160S, at pH 8.5 and 20°C
410
-
mutant enzyme Y229F, at pH 8.5 and 20°C
130
-
mutant enzyme Y229S, at pH 8.5 and 20°C
350
-
pH 8.0, 37°C
94.2
-
pH 8.5, 37°C
49
-
pH 9.0, 10°C
382
-
pH 9.0, 15°C
546
-
pH 9.0, 20°C
694
-
pH 9.0, 25°C
750
-
pH 9.0, 30°C
690
-
pH 9.0, 5°C
235
-
wild type enzyme, at pH 8.5 and 20°C
440
-
Y227C/E277G double mutant, at 30°C
2200
-
Y227C/E277G double mutant, at 55°C
3500
-
25°C, pH 9.5
0.82
-
-
0.0333
-
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
20.7
-
pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme
22.6
-
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
38.4
-
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
34.9
-
pH 8.0, 37°C
4.3
-
pH 8.0, 37°C, recombinant wild-type enzyme
2.1
-
recombinant mutant R180Tenzyme, pH 8.0, 25°C
0.37
-
recombinant wild-type enzyme, pH 8.0, 25°C
34.5
-
pH 8.0, 65°C
2.44
-
pH 8.0, temperature not specified in the publication
3.5
-
30°C, pH 5.5
30°C, pH 7.5
0.14
-
circular dichroism assay, pH 7.8, 25°C
4.2
-
CO2 assay, pH 7.8, 25°C
3.3
-
mutant E165A, pH 7.0, temperature not specified in the publication
4.8
-
mutant E165G, pH 7.0, temperature not specified in the publication
5.6
-
mutant E165S, pH 7.0, temperature not specified in the publication
10.1
-
mutant E165T, pH 7.0, temperature not specified in the publication
24.8
-
mutant E165V, pH 7.0, temperature not specified in the publication
10.9
-
mutant enzyme D364E, at pH 7.5 and 37°C
0.015
-
mutant enzyme S396A, at pH 7.5 and 37°C
10
-
mutant I163A, pH 7.0, temperature not specified in the publication
3.6
-
mutant I163G, pH 7.0, temperature not specified in the publication
4.2
-
mutant I163S, pH 7.0, temperature not specified in the publication
7.4
-
mutant I163T, pH 7.0, temperature not specified in the publication
10.1
-
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
38.5
-
mutant I163V, pH 7.0, temperature not specified in the publication
4.4
-
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
25.7
-
mutant K294A, pH 8.0, 37°C
3.5
-
pH 5.5, 37°C
9.77
-
pH 8.0, 22°C
0.18
-
recombinant Pf-Hinge-ODC
0.006
-
recombinant PfODC domain
0.003
-
wild type enzyme, at pH 7.5 and 37°C
7
-
wild-type, pH 7.0, temperature not specified in the publication
3.4
-
wild-type, pH 8.0, 37°C
15.4
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
8.4
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
14
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
4.8
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
3
6
pH 6.0, 30°C, mutant enzyme A52C
7
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
7.2
-
pH 6.0, 30°C, mutant enzyme G319W
7.2
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4.7
-
pH 6.0, 30°C, mutant enzyme P54D
13
-
pH 6.0, 30°C, mutant enzyme S322A
20
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
24
-
pH 6.0, 30°C, wild type enzyme
8.6
-
pH 6.0, 40°C
289.8
-
at pH 7.5, 70°C
0.04
-
DABA AT/DC fusion protein
0.54
-
mutant F344H, pH 7.5, 37°C
2.3
-
mutant F344Y, pH 7.5, 37°C
0.4
-
mutant M341L, pH 7.5, 37°C
0.29
-
pH 7.5, 37°C
pH 7.5, 37°C, recombinant enzyme
2.78
-
wild-type, pH 7.5, 37°C
0.91
-
-
1660
-
pH 8.5, room temperature
980
-
pH 8.0, 30°C, recombinant wild-type enzyme
1.83
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
68.8
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
87.7
-

KM Value (300 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
dehydrogenation with phenazine methosulfate
0.42
-
oxidation with O2
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
18
-
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
16
-
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
15
-
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
12
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
21
-
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
18
-
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
1.1
-
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
1
-
pH 8.0, 25°C
0.286
-
pH 8.0, 25°C, recombinant detagged enzyme
0.058
-
pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine
1.7
-
pH 7.5, 25°C, cosubstrate: NADH, oxygen consumption assay
0.5
-
pH 7.5, 25°C, cosubstrate: NADPH, following the formation of hydroxylated ornithine
1.7
-
pH 7.5, 25°C, cosubstrate: NADPH, oxygen consumption assay
2
-
pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH
0.21
-
pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH
0.3
-
recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication
0.107
-
recombinant holo-enzyme, pH 7.5, temperature not specified in the publication
0.305
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.33
-
at pH 8.0 and 20°C, measured at the rate of H2O2 production
0.017
-
at pH 8.5 and 30°C
5.6
-
fraction II
14.2
-
pH 7.6, 30°C
brain enzyme
25
-
with pyruvate and NADPH as cosubstrates
0.7
-
pH 7.5, temperature not specified in the publication
29.5
-
-
0.85
-
37°C, pH 8.2
0.33
-
37°C, pH 8.6
0.25
-
37°C, pH 9.0
0.45
-
liver enzyme, pH 7.0
0.00232
-
liver enzyme, presence of putrescine, pH 7.0
0.001
-
mutant arcB6240, pH 7.25
1.85
-
mutant arcB6254, pH 7.25
1.8
-
mutant C191M/C194N/F197V, pH 8.0, 30°C
2.8
-
mutant D182N, pH 8.0, 30°C
49
-
mutant E123A, pH 8.0, 30°C
2.6
-
mutant E123S, pH 8.0, 30°C
2.1
-
mutant E256A, pH 8.0, 30°C
10
-
mutant E256Q, pH 8.0, 30°C
1.2
-
mutant enzyme C273A, at pH 8.5 and 20°C
0.73
-
mutant enzyme D140N, at pH 8.5 and 20°C
17
-
mutant enzyme D231A, at pH 8.5 and 20°C
0.59
-
mutant enzyme E299D, at pH 8.5 and 20°C
0.9
-
mutant enzyme E299Q, at pH 8.5 and 20°C
0.33
-
mutant enzyme H272L, at pH 8.5 and 20°C
0.68
-
mutant enzyme H272N, at pH 8.5 and 20°C
0.4
-
mutant enzyme Q104L, at pH 8.5 and 20°C
0.81
-
mutant enzyme R57A, at pH 8.5 and 20°C
0.44
-
mutant enzyme S61A, at pH 8.5 and 20°C
0.53
-
mutant enzyme Y160F, at pH 8.5 and 20°C
1
-
mutant enzyme Y160S, at pH 8.5 and 20°C
7.3
-
mutant enzyme Y229F, at pH 8.5 and 20°C
0.45
-
mutant enzyme Y229S, at pH 8.5 and 20°C
0.61
-
mutant K260A, pH 8.0, 30°C
1
-
mutant K260R, pH 8.0, 30°C
1.2
-
mutant K263A, pH 8.0, 30°C
30
-
mutant K263R, pH 8.0, 30°C
20
-
mutant K265A, pH 8.0, 30°C
1.2
-
mutant K265R, pH 8.0, 30°C
1.1
-
mutant K268A, pH 8.0, 30°C
0.05
-
mutant K268R, pH 8.0, 30°C
1.1
-
mutant K289S, pH 8.0, 30°C
10
-
mutant K88Q, pH 7.7, 37°C
0.55
-
mutant K88R, pH 7.7, 37°C
0.42
-
mutant L290Q, pH 8.0, 30°C
2
-
mutant L290S, pH 8.0, 30°C
2
-
mutant N184Q, pH 8.0, 30°C
34
-
mutant N185Q, pH 8.0, 30°C
350
-
mutant Q294P, pH 8.0, 30°C
1.3
-
mutant T68G, pH 8.0, 30°C
3.4
-
pH 8.0, 37°C
pH 8.5, 10 mM fixed substrate
0.85
-
pH 8.5, 37°C
1.1
-
pH 9.0, 10°C
3.34
-
pH 9.0, 15°C
5.67
-
pH 9.0, 20°C
8
-
pH 9.0, 25°C
22.49
-
pH 9.0, 30°C
45
-
pH 9.0, 5°C
1.78
-
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C
32
-
recombinant wild-type enzyme, pH 8.5, 37°C
36.4
-
wild type enzyme, at pH 8.5 and 20°C
0.53
-
wild type, pH 7.25
0.8
-
wild-type, pH 7.7, 37°C
0.36
-
wild-type, pH 8.0, 30°C
1.6
-
25°C, pH 9.5
0.64
-
25°C, pH 8.0
2
-
37°C
2
-
AH 130 cells, pH 7.5
2
-
assay based on detection of L-glutamate, pH 8.0, 37°C
8.97
-
assay based on reduction of DELTA1-pyrroline-5-carboxylate, pH 8.0, 37°C
10.5
-
gut, pH 7.5
1.113
-
in rat brain mitochondrial fraction, in absence of pyridoxal 5'-phosphate
2.089
-
in rat brain mitochondrial fraction, in presence of 0.05 mM pyridoxal 5'-phosphate
5.089
-
kidney, pH 7.5
liver, pH 7.5
1.4
-
normal conditions
91
-
pH 7.4, 37°C
3.95
-
pH 7.6, 37°C
6.2
-
pH 7.8, 37°C
pH 8, 37°C
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
6.9
-
pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme
7
-
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
5.1
-
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
6.5
-
pH 8.0, 37°C
15
-
pH 8.0, 37°C, recombinant wild-type enzyme
6.9
-
pH 8.5, 37°C
1.8
-
pH and temperature not specified in the publication
pH and temperature not specified in the publication, brain enzyme
1.1
-
pH and temperature not specified in the publication, enzyme from astrocytes
4.3
-
pH and temperature not specified in the publication, enzyme from cerebellar granule cells
4.7
-
pH and temperature not specified in the publication, enzyme from cortical interneurons
0.8
-
pH and temperature not specified in the publication, eye enzyme
5.6
-
pH and temperature not specified in the publication, eye retina enzyme
3.7
-
pH and temperature not specified in the publication, kidney enzyme
0.59
-
pH and temperature not specified in the publication, liver enzyme
pH and temperature not specified in the publication, liver isolated mitochondria
4
-
pH and temperature not specified in the publication, small intestine enzyme
0.6
-
poorly differentiated gastroadenocarcinoma, pH 7.5
3.275
-
recombinant mutant R180Tenzyme, pH 8.0, 25°C
2
37
recombinant wild-type enzyme, pH 8.0, 25°C
6.5
-
rhinopharyngeal tumor, pH 7.5
1.7
-
salt stress conditions
87
-
transgenic mouse, pH 7.5, 37°C
15.32
-
well differentiated gastroadenocarcinoma, pH 7.5
1.282
-
wild-type (OAT in parasite cell extract), pH 7.4, 37°C
2.3
-
wild-type with PfGrx, pH 7.4, 37°C
1.5
-
wild-type with PfTrx, pH 7.4, 37°C
0.9
-
wild-type, pH 7.4, 37°C
1.6
-
wild-type, pH 7.5, 37°C
13.94
-
with 2-oxoglutarate as cosubstrate, pH 7.1, 37°C
2.8
-
with glyoxylate as cosubstrate, pH 7.1, 37°C
2.9
-
with pyruvate as cosubstrate, pH 7.1, 37°C
1.7
-
-
2.9
-
pH 8.0, 37°C
2
-
pH 8.0, 65°C
7.95
-
pH 8.0, temperature not specified in the publication
4.391
-
30°C, pH 5.5
30°C, pH 7.5
7.2
-
apparent value, at 37°C
0.4
-
at pH 5.5, 35°C
1
-
biosynthetic ornithine decarboxylase
5.6
-
C115A mutant
1.79
-
C360A mutant
0.1
-
C360S mutant
0.054
-
circular dichroism assay, pH 7.8, 25°C
0.214
-
CO2 assay, pH 7.8, 25°C
0.122
-
cytosolic enzyme
2.2
-
degradative ornithine decarboxylase
3.6
-
enzyme from chromatin
1
-
enzyme from epidermis
0.07
-
in 10 mM sodium phosphate buffer, pH 7.0
0.06
-
in absence of NaCl
0.1
-
in presence of 0.25 M NaCl
in presence of 2.9 mM dithiothreitol
0.09
-
K69R mutant
0.18
-
larva, 37°C, pH 7.1
438
-
mutant E165A, pH 7.0, temperature not specified in the publication
2.4
-
mutant E165G, pH 7.0, temperature not specified in the publication
3
-
mutant E165S, pH 7.0, temperature not specified in the publication
1.9
-
mutant E165T, pH 7.0, temperature not specified in the publication
0.7
-
mutant E165V, pH 7.0, temperature not specified in the publication
1.4
-
mutant enzyme C360A
0.03
-
mutant enzyme C70S
0.15
-
mutant enzyme D364E, at pH 7.5 and 37°C
55.2
-
mutant enzyme K69A
0.081
-
mutant enzyme S396A, at pH 7.5 and 37°C
0.27
-
mutant I163A, pH 7.0, temperature not specified in the publication
1.5
-
mutant I163G, pH 7.0, temperature not specified in the publication
1.7
-
mutant I163S, pH 7.0, temperature not specified in the publication
1.5
-
mutant I163T, pH 7.0, temperature not specified in the publication
0.6
-
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
0.6
-
mutant I163V, pH 7.0, temperature not specified in the publication
1.3
-
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
1.1
-
mutant K294A, pH 8.0, 37°C
43
-
native enzyme
0.28
-
ovaries of young females, 37°C, pH 7.1
1660
-
pH 5.5, 37°C
1.6
-
pH 7.3, 37°C
0.19
-
pH 8.0, 22°C
0.395
-
pupa, 37°C, pH 7.1
207
-
recombinant enzyme
0.33
-
recombinant Pf-Hinge-ODC
0.047
-
recombinant PfODC
0.041
-
recombinant PfODC domain
0.16
-
wild type enzyme
0.086
-
wild type enzyme, at pH 7.5 and 37°C
0.37
-
wild-type, pH 7.0, temperature not specified in the publication
3.3
-
wild-type, pH 8.0, 37°C
0.37
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
0.98
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
3.1
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
4
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
3.3
-
pH 6.0, 30°C, mutant enzyme A52C
1.3
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
1.6
-
pH 6.0, 30°C, mutant enzyme G319W
1.3
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4.5
-
pH 6.0, 30°C, mutant enzyme P54D
2.1
-
pH 6.0, 30°C, mutant enzyme S322A
1.2
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
1.5
-
pH 6.0, 30°C, wild type enzyme
0.96
-
pH 6.0, 40°C
1.2
-
at pH 7.5, 70°C
7.5
-
pH 8.2, 37°C
180
-
pH 9.0, 40°C
46
-
DABA AT/DC fusion protein
11.1
-
mutant F344H, pH 7.5, 37°C
1.53
-
mutant F344Y, pH 7.5, 37°C
1.59
-
mutant M341L, pH 7.5, 37°C
1.04
-
pH 7.5, 37°C
pH 7.5, 37°C, recombinant enzyme
1.43
-
wild-type, pH 7.5, 37°C
1.05
-
-
11.1
-
0.5 mM NAD+ and 0.1 mM L-arginine, strain GR4
2
-
0.5 mM NAD+, in the absence of L-arginine
1.7
-
0.5 mM NAD+, in the presence of L-arginine
0.25
-
crude extracts
5
-
in the absence of ADP
5.5
-
in the absence of L-arginine , OCD, C58
1.7
-
in the presence of ADP
6.2
-
OCD, Ach5, in the absence of L-arginine
0.25
-
OCD, C58, in the presence of L-arginine
0.25
-
-
0.9
-
D-Lys
0.9
-
L-Orn
0.9
-
-
0.52
-
pH 8.5, room temperature
0.77
-
pH 8.0, 30°C, recombinant wild-type enzyme
27
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3.7
-
pH 7.5, 37°C
at 68°C
27
-

Ki Value (30 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
pH 7.4
5.4
-
pH 7.6, 30°C
at pH 7.0
5
-
at 10 mM carbamoyl phosphate
3.6
-
at 2 mM carbamoyl phosphate
1.7
-
pH 8.5, 37°C
1.9
-
pH 8.5, 30°C
0.25
-
-
0.46
-
pH 7.8, 35°C, mixed inhibition
9.5
-
pH 7.8, 35°C, competitive inhibition with respect to 2-oxoglutarate
5.6
-
forward reaction with 4-aminobutanoate and pyruvate, pH 9.0, 30°C
0.46
-
pH 8.5
4.3
-
pH 9.5, 37°C, liver enzyme
1.4
-
wild type enzyme
1
-
product inhibition constant, Mn2+-activated mutant S230G, pH 7.4, 37°C
0.7
-
product inhibition constant, Mn2+-activated mutant D181N/S230G, pH 7.4, 37°C
1
-
product inhibition constant, Mn2+-activated mutant D181N, pH 7.4, 37°C
2.4
-
product inhibition constant, Co2+-activated mutant S230G, pH 7.4, 37°C
0.05
-
product inhibition constant, Co2+-activated mutant D181N/S230G, pH 7.4, 37°C
0.09
-
product inhibition constant, Co2+-activated mutant D181N, pH 7.4, 37°C
0.11
-
presence of 0.1 mM Mn2+, pH 9.4, 37°C
0.7
-
pH 7.5, 37°C
30
-
pH 9.5, 37°C, enzyme from submandibular gland
7.8
-
pH 9.4, 37°C
1.18
-
at pH 7.0 and 30°C
2.16
-
mutant enzyme N130D
7.8
-
pH 10, 37°C
1.9
-

IC50 Value (7 results)

COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
pH 7.5, 30°C
5
-
pH 8.0, 30°C
2.4
-
pH 7.5, 22°C, recombinant wild-type enzyme
5
-
-
2
-
IC50 above 70 mM
70
-
pH 7.5, 37°C
24
-
pH 8.5, 21°C
0.7
-

References & Links