BRENDA - Enzyme Database show
show all sequences of 1.13.12.2

Regulation of a catabolic pathway. Lysine degradation in Pseudomonas putida

Vandecasteele, J.P.; Hermann, M.; Eur. J. Biochem. 31, 80-85 (1972)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
KCl
activation
Pseudomonas putida
NaCl
activation
Pseudomonas putida
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
60% inhibition at 5 mM
Pseudomonas putida
5-Aminovaleramide
42% inhibition at 5 mM
Pseudomonas putida
5-Aminovalerate
36% inhibition at 5 mM
Pseudomonas putida
acetate
38% inhibition at 5 mM
Pseudomonas putida
citrate
76% inhibition at 5 mM
Pseudomonas putida
glutamate
42% inhibition at 5 mM
Pseudomonas putida
Glutarate
57% inhibition at 5 mM
Pseudomonas putida
Mg2+
56% inhibition at 1 mM
Pseudomonas putida
oxaloacetate
67% inhibition at 5 mM
Pseudomonas putida
succinate
52% inhibition at 5 mM
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-Lysine + O2
Pseudomonas putida
L-lysine degradation
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-Lysine + O2
L-lysine degradation
440273
Pseudomonas putida
?
-
-
-
?
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
KCl
activation
Pseudomonas putida
NaCl
activation
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
60% inhibition at 5 mM
Pseudomonas putida
5-Aminovaleramide
42% inhibition at 5 mM
Pseudomonas putida
5-Aminovalerate
36% inhibition at 5 mM
Pseudomonas putida
acetate
38% inhibition at 5 mM
Pseudomonas putida
citrate
76% inhibition at 5 mM
Pseudomonas putida
glutamate
42% inhibition at 5 mM
Pseudomonas putida
Glutarate
57% inhibition at 5 mM
Pseudomonas putida
Mg2+
56% inhibition at 1 mM
Pseudomonas putida
oxaloacetate
67% inhibition at 5 mM
Pseudomonas putida
succinate
52% inhibition at 5 mM
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-Lysine + O2
Pseudomonas putida
L-lysine degradation
?
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-Lysine + O2
L-lysine degradation
440273
Pseudomonas putida
?
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-
?
Other publictions for EC 1.13.12.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745567
Wang
-
Efficient production of 5-ami ...
Pseudomonas putida
J. Mol. Catal. B
134
115-121
2016
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745703
Rohles
Systems metabolic engineering ...
Pseudomonas putida
Microb. Cell Fact.
15
154
2016
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745704
Shin
Metabolic engineering of Cory ...
Pseudomonas putida, Pseudomonas putida ATCC 12633
Microb. Cell Fact.
15
174
2016
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1
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746458
Li
Overexpression of transport p ...
Pseudomonas putida
Sci. Rep.
6
30884
2016
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1
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4
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1
1
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742530
Matsui
Mutational and crystallograph ...
Pseudomonas sp. AIU 813
FEBS Open Bio
4
220-228
2014
-
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1
1
18
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1
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2
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2
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1
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3
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5
1
1
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1
1
1
18
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1
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1
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3
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5
1
1
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1
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2
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744567
Park
High-level conversion of L-ly ...
Pseudomonas putida
Biotechnol. J.
9
1322-1328
2014
-
1
1
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1
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3
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1
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746434
Liu
Enzymatic production of 5-ami ...
Pseudomonas putida
Sci. Rep.
4
5657
2014
-
1
1
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1
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1
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3
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1
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1
1
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1
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1
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1
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1
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1
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1
1
1
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1
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2
2
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728239
Park
Metabolic engineering of Esche ...
Pseudomonas putida
Metab. Eng.
16
42-47
2013
-
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1
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4
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2
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440262
Karyakin
-
Kinetic properties of L-lysine ...
Pseudomonas putida
Prikl. Biokhim. Mikrobiol.
27
825-832
1991
-
1
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440263
Simonyan
-
A flow-through enzyme analyzer ...
Pseudomonas putida
Biosens. Bioelectron.
6
93-99
1991
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1
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440264
Ohnishi
Studies on the reaction specif ...
Pseudomonas fluorescens
Arch. Biochem. Biophys.
176
358-365
1976
3
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3
1
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1
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10
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440265
Maruyama
A dehydrogenase reaction catal ...
Pseudomonas fluorescens
Arch. Biochem. Biophys.
173
480-489
1976
1
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1
10
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10
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10
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440266
Yamauchi
A possible involvement of sulf ...
Pseudomonas fluorescens
J. Biol. Chem.
250
7127-7133
1975
1
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2
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1
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440267
Yamamoto
Alkylamine-dependent oxidation ...
Pseudomonas fluorescens
Arch. Biochem. Biophys.
171
316-326
1975
1
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1
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1
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390102
Flashner
-
Flavoprotein oxygenases ...
Pseudomonas fluorescens
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
245-283
1974
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2
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1
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440269
Flashner
Regulatory properties of the f ...
Pseudomonas fluorescens
J. Biol. Chem.
249
2587-2592
1974
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1
4
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440270
Flashner
Purification and properties of ...
Pseudomonas fluorescens
J. Biol. Chem.
249
2579-2586
1974
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1
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2
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1
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440271
Yamauchi
Reversible conversion of lysin ...
Pseudomonas fluorescens
J. Biol. Chem.
248
3750-3752
1973
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2
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1
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440272
Yamamoto
Alkylamine-dependent amino-aci ...
Pseudomonas fluorescens
Proc. Natl. Acad. Sci. USA
69
3723-3726
1972
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440273
Vandecasteele
Regulation of a catabolic path ...
Pseudomonas putida
Eur. J. Biochem.
31
80-85
1972
2
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10
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440274
Nakazawa
Studies on monooxygenases. V. ...
Pseudomonas fluorescens
J. Biol. Chem.
247
3439-3444
1972
1
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5
5
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1
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8
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5
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5
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8
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1
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440275
Yamamoto
Studies on monooxygenases. IV. ...
Pseudomonas fluorescens
J. Biol. Chem.
247
3434-3438
1972
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440276
Nakazawa
-
Lysine oxygenase (Pseudomonas) ...
Pseudomonas fluorescens
Methods Enzymol.
17B
154-157
1971
-
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1
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4
1
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1
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1
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1
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1
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1
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440277
Yamamoto
Studies on monooxygenases. III ...
Pseudomonas fluorescens
J. Biol. Chem.
244
2951-2955
1969
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1
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440278
Takeda
Studies on monooxygenases. I. ...
Pseudomonas fluorescens
J. Biol. Chem.
244
2935-2941
1969
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4
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1
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1
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3
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1
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1
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4
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1
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3
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1
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1
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1
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440279
Takeda
Crystalline L-lysine oxygenase ...
Pseudomonas fluorescens
J. Biol. Chem.
241
2733-2736
1966
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1
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