BRENDA - Enzyme Database show
show all sequences of 1.5.3.7

Mechanism-based inactivity of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-thia-L-pipecolic acid

Zabriskie, T.M.; Liang, X.; Bioorg. Med. Chem. Lett. 7, 457-462 (1997)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
(S)-1,3-thiazane-4-carboxylic acid
causes time-dependent, irreversible, stereospecific inactivation
Macaca mulatta
L-homocysteine
at 0.005 mM 12% inactivation after 1 h incubation
Macaca mulatta
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.5
-
L-pipecolic acid
-
Macaca mulatta
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
peroxisome
membrane-associated
Macaca mulatta
5777
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
1 * 46000, SDS-PAGE
Macaca mulatta
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-pipecolate + O2
Macaca mulatta
-
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
the product reacts with water to form 2-aminoadipate 6-semialdehyde
Macaca mulatta
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Macaca mulatta
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1,3-thiazane-4-carboxylic acid + O2
-
392471
Macaca mulatta
? + H2O2
-
-
-
?
L-pipecolate + O2
-
392471
Macaca mulatta
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
the product reacts with water to form 2-aminoadipate 6-semialdehyde
392471
Macaca mulatta
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 46000, SDS-PAGE
Macaca mulatta
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
covalently bound
Macaca mulatta
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
36
-
(S)-1,3-thiazane-4-carboxylic acid
competitive inhibitor that completely inactivates the enzyme
Macaca mulatta
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
covalently bound
Macaca mulatta
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(S)-1,3-thiazane-4-carboxylic acid
causes time-dependent, irreversible, stereospecific inactivation
Macaca mulatta
L-homocysteine
at 0.005 mM 12% inactivation after 1 h incubation
Macaca mulatta
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
36
-
(S)-1,3-thiazane-4-carboxylic acid
competitive inhibitor that completely inactivates the enzyme
Macaca mulatta
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.5
-
L-pipecolic acid
-
Macaca mulatta
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
peroxisome
membrane-associated
Macaca mulatta
5777
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
1 * 46000, SDS-PAGE
Macaca mulatta
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-pipecolate + O2
Macaca mulatta
-
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
the product reacts with water to form 2-aminoadipate 6-semialdehyde
Macaca mulatta
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1,3-thiazane-4-carboxylic acid + O2
-
392471
Macaca mulatta
? + H2O2
-
-
-
?
L-pipecolate + O2
-
392471
Macaca mulatta
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
the product reacts with water to form 2-aminoadipate 6-semialdehyde
392471
Macaca mulatta
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 46000, SDS-PAGE
Macaca mulatta
Other publictions for EC 1.5.3.7
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)
742960
Natarajan
Evidence for pipecolate oxida ...
Homo sapiens
J. Cell. Biochem.
118
1678-1688
2017
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1
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2
2
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743036
Posset
Understanding cerebral L-lysi ...
Mus musculus
J. Inherit. Metab. Dis.
38
265-272
2015
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656324
Yoshida
Characterization of two fructo ...
Schizosaccharomyces pombe
J. Biosci. Bioeng.
97
278-280
2004
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1
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2
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1
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4
1
1
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1
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392467
Naranjo
Conversion of pipecolic acid i ...
Penicillium chrysogenum
J. Bacteriol.
183
7165-7172
2001
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1
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7
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392469
Dodt
The human L-pipecolic acid oxi ...
Homo sapiens
Cell Biochem. Biophys.
32
313-316
2000
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1
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392470
Ijlst
Molecular cloning and expressi ...
Homo sapiens
Biochem. Biophys. Res. Commun.
270
1101-1105
2000
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1
1
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1
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4
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1
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1
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1
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392471
Zabriskie
-
Mechanism-based inactivity of ...
Macaca mulatta
Bioorg. Med. Chem. Lett.
7
457-462
1997
-
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-
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-
2
1
1
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1
1
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1
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2
1
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1
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1
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392472
Zabriskie
-
Stereochemical course of the o ...
Macaca mulatta
J. Am. Chem. Soc.
119
6446-6447
1997
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392473
Rao
L-Pipecolic acid oxidation in ...
Rattus norvegicus
Biochim. Biophys. Acta
1164
29-35
1993
2
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2
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2
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392475
Rao
L-Pipecolic acid metabolism in ...
Homo sapiens
Biochim. Biophys. Acta
1038
295-299
1990
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2
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392476
Wanders
L-pipecolate oxidase: a distin ...
Homo sapiens
Biochem. Biophys. Res. Commun.
164
550-555
1989
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1
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2
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392477
Mihalik
L-Pipecolic acid oxidation in ...
Macacine alphaherpesvirus 1, Oryctolagus cuniculus
J. Biol. Chem.
264
2509-2517
1989
1
2
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4
2
2
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392478
Kinzel
Lysine biosynthesis in Rhodoto ...
Rhodotorula glutinis
J. Bacteriol.
151
1073-1077
1982
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1
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