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EC Tree
IUBMB Comments The product reacts with water to form (S)-2-amino-6-oxohexanoate.
The enzyme appears in viruses and cellular organisms
Synonyms
pipox, l-pipecolate oxidase, pipecolate oxidase,
more
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L-pipecolic acid oxidase
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pipecolate oxidase
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L-pipecolate oxidase
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L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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L-pipecolate:oxygen 1,6-oxidoreductase
The product reacts with water to form (S)-2-amino-6-oxohexanoate.
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(S)-1,3-thiazane-4-carboxylic acid + O2
? + H2O2
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-
-
-
?
L-pipecolate + O2
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
additional information
?
-
L-pipecolate + O2
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
-
?
L-pipecolate + O2
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
pipecolate metabolism leads to protection against H2O2 stress in mammalian cells. The enzyme is necessary for pipecolate protection
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-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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the pro-6(R)-hydrogen of pipecolic acid is removed stereospecifically
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
-
-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
-
-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
-
-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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highly specific for
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?
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
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?
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
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?
L-proline + O2
?
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?
L-proline + O2
?
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low activity
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?
additional information
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enzyme is involved in L-lysine metabolism
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?
additional information
?
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no activity with fructosyl-amino acids, L-saccharopine, and sarcosine
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?
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L-pipecolate + O2
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
pipecolate metabolism leads to protection against H2O2 stress in mammalian cells. The enzyme is necessary for pipecolate protection
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-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
additional information
?
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enzyme is involved in L-lysine metabolism
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?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
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-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
-
the product reacts with water to form 2-aminoadipate 6-semialdehyde
?
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
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-
-
?
L-pipecolate + O2
DELTA1-piperideine-6-carboxylate + H2O2
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-
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?
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FAD
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FAD
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covalently attached
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(S)-1,3-thiazane-4-carboxylic acid
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causes time-dependent, irreversible, stereospecific inactivation
HgCl2
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100% inhibition at 1 mM
hydroxylamine
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15% inhibition at 1 mM
KCN
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20% inhibition at 1 mM
L-homocysteine
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at 0.005 mM 12% inactivation after 1 h incubation
p-chloromercuribenzoate
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100% inhibition at 1 mM
phenazine ethosulfate
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antimycin A
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L-proline
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L-proline
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competitive inhibitor
rotenone
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di-(2-ethylhexyl)phthalate
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5 g per kg body weight, 500% activity enhancement in the peroxisomal fraction
glucagon
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3 mg per kg body weight, 150% activity enhancement in the mitochondrial fraction
additional information
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activity is maximal when FAD, phenazine ethosulfate and glycerol are included in the assay
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Breast Neoplasms
Human snoRNA-93 is processed into a microRNA-like RNA that promotes breast cancer cell invasion.
Genetic Diseases, Inborn
Peroxisomal oxidation of pipecolic acid in the rat.
Neoplasm Metastasis
Expression of sarcosine metabolism-related proteins according to metastatic site in breast cancer.
Peroxisomal Disorders
Assay for L-pipecolate oxidase activity in human liver: detection of enzyme deficiency in hyperpipecolic acidaemia.
Zellweger Syndrome
Assay for L-pipecolate oxidase activity in human liver: detection of enzyme deficiency in hyperpipecolic acidaemia.
Zellweger Syndrome
Identification of L-pipecolate oxidase in human liver and its deficiency in the Zellweger syndrome.
Zellweger Syndrome
Peroxisomal oxidation of pipecolic acid in the rat.
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4.07
L-pipecolate
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pH 8.0, 30°C, recombinant enzyme
0.74 - 6
L-pipecolic acid
3 - 3.5
L-proline
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pH 8.0, 30°C, recombinant enzyme
0.74
L-pipecolic acid
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-
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36
(S)-1,3-thiazane-4-carboxylic acid
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competitive inhibitor that completely inactivates the enzyme
10
L-proline
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-
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0.002
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strain Wis 54-1255, HS1-, 10.25
additional information
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-
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8.5
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-
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brenda
cynomolgus monkey
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strains Wis 54-1255, HS1-, and 10.25
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male sprague-dawley rats
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strains wild-type, MU-1 and lys5
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gene FAP1
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SwissProt
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brenda
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additional information
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not detected in liver
brenda
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brenda
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white matter contains a more than 2-fold higher activity than cortex
brenda
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highest activity in the kidney cortex
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highest activity in the kidney cortex
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brenda
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brenda
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soluble fraction
brenda
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matrix protein
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membrane-associated
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membrane-associated
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brenda
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membrane-associated
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malfunction
knockdown of the enzyme by small interference RNA abolishes pipecolate protection against hydrogen peroxide-induced cell death in HEK293 cells suggesting a critical role for this enzyme
physiological function
pipecolate metabolism leads to protection against H2O2 stress in mammalian cells. The enzyme is necessary for pipecolate protection
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SOX_BOVIN
392
0
43820
Swiss-Prot
other Location (Reliability: 2 )
SOX_HUMAN
390
1
44066
Swiss-Prot
other Location (Reliability: 2 )
SOX_MOUSE
390
0
43847
Swiss-Prot
other Location (Reliability: 2 )
SOX_RABIT
390
1
44122
Swiss-Prot
other Location (Reliability: 2 )
Y9130_DICDI
1080
0
120674
Swiss-Prot
other Location (Reliability: 2 )
SWNR_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
305
0
34471
Swiss-Prot
other Location (Reliability: 2 )
SWNR_METRA
Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075)
305
0
34289
Swiss-Prot
other Location (Reliability: 2 )
FAP1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
412
1
46320
Swiss-Prot
Secretory Pathway (Reliability: 3 )
A0A0A1I4W9_9PSED
427
0
46348
TrEMBL
-
A0A198UFQ1_MORCA
430
0
47824
TrEMBL
-
A0A081G2J5_9GAMM
441
0
47903
TrEMBL
-
A0A5B7AAM8_DAVIN
433
0
46376
TrEMBL
other Location (Reliability: 5 )
A0A2Z4LNS7_9FLAO
Muricauda aurantiaca
399
0
45096
TrEMBL
-
D4XAM0_9BURK
429
0
46154
TrEMBL
-
A0A1Z5JET4_FISSO
409
0
45481
TrEMBL
other Location (Reliability: 3 )
L8MFQ0_PSEFK
428
0
46600
TrEMBL
-
A0A3G9G2I2_9CAUL
429
0
45683
TrEMBL
-
A0A0A8TP43_ACIBZ
427
0
47069
TrEMBL
-
A0A481V2Q7_9CAUD
115
0
11854
TrEMBL
Mitochondrion (Reliability: 4 )
L8MGA4_PSEFK
427
0
46376
TrEMBL
-
A0A3B0SI08_9ZZZZ
422
0
44388
TrEMBL
other Location (Reliability: 3 )
W1QG18_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
428
0
48045
TrEMBL
Secretory Pathway (Reliability: 4 )
A0A2I0A787_9ASPA
423
0
45143
TrEMBL
other Location (Reliability: 4 )
A0A2I0A793_9ASPA
443
0
48030
TrEMBL
other Location (Reliability: 3 )
A0A063XWB3_9GAMM
426
0
46161
TrEMBL
-
A0A654KF14_TAYEM
Taylorella equigenitalis (strain MCE9)
431
0
47474
TrEMBL
-
S9RW06_9RHOB
421
0
44730
TrEMBL
-
A0A7Z0UWL8_MORCA
430
0
47853
TrEMBL
-
Q88CC4_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
432
0
47023
TrEMBL
-
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43000
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1 * 43000, SDS-PAGE
46000
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1 * 46000, SDS-PAGE
56000
-
2 * 56000, about, recombinant enzyme, SDS-PAGE
98000
-
recombinant enzyme, gel filtration
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?
x * 44000, calculated from amino acid sequence
dimer
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2 * 56000, about, recombinant enzyme, SDS-PAGE
monomer
-
1 * 46000, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
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45
-
10 min 20% activity, bovine serum albumin at 1 mg per ml protects from thermal inactivation
53
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complete inactivation
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-70°C, Tris-HCl buffer pH 8.7, 1 mM 2-mercaptoethanol, several weeks, 100% activity
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4°C, Tris-HCl buffer pH 8.7, 1 mM 2-mercaptoethanol, several days, 100% activity
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recombinant enzyme from Escherichia coli strain JM109
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DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
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expressed as a chimera between maltose-binding protein and L-pipecolic acid oxidase
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expressed in Escherichia coli BL21
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expressed in Escherichia coli DH10B
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medicine
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L-pipecolic acid is formed by the catabolism of lysine in humans, and its accumulation is one of the first biochemical abnormalities detected in the Zellweger syndrome
medicine
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L-pipecolic oxidase activity is deficient in patients with peroxisome biogenesis disorders
medicine
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L-pipecolic oxidase activity is deficient in patients with peroxisome biogenesis disorders
medicine
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L-pipecolic oxidase activity is deficient in patients with peroxisome biogenesis disorders
medicine
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the L-pipecolate pathway for degradation of lysine is the principal one in the brain
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Naranjo, L.; Martin de Valmaseda, E.; Banuelos, O.; Lopez, P.; Riano, J.; Casqueiro, J.; Martin, J.F.
Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase
J. Bacteriol.
183
7165-7172
2001
Penicillium chrysogenum
brenda
Dodt, G.; Kim, D.; Reimann, S.; McCabe, K.; Gould, S.J.; Mihalik, S.J.
The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases
Cell Biochem. Biophys.
32
313-316
2000
Homo sapiens
brenda
Ijlst, L.; de Kromme, I.; Oostheim, W.; Wanders, R.J.A.
Molecular cloning and expression of human L-pipecolate oxidase
Biochem. Biophys. Res. Commun.
270
1101-1105
2000
Homo sapiens
brenda
Zabriskie, T.M.; Liang, X.
Mechanism-based inactivity of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-thia-L-pipecolic acid
Bioorg. Med. Chem. Lett.
7
457-462
1997
Macaca mulatta
-
brenda
Zabriskie, T.M.; Kelly, W.L.; Liang, X.
Stereochemical course of the oxidation of L-pipecolic acid by the flavoenzyme L-pipecolate oxidase
J. Am. Chem. Soc.
119
6446-6447
1997
Macaca mulatta
-
brenda
Rao, V.V.; Tsai, M.J.; Pan, X.; Chang, Y.F.
L-Pipecolic acid oxidation in rat: subcellular localization and developmental study
Biochim. Biophys. Acta
1164
29-35
1993
Rattus norvegicus
brenda
Rao, V.V.; Chang, Y.F.
L-Pipecolic acid metabolism in human liver: detection of L-pipecolate oxidase and identification of its reaction product
Biochim. Biophys. Acta
1038
295-299
1990
Homo sapiens
brenda
Wanders, R.J.A.; Romeyn, G.J.; Schutgens, R.B.H.; Tager, J.M.
L-pipecolate oxidase: a distinct peroxisomal enzyme in man
Biochem. Biophys. Res. Commun.
164
550-555
1989
Homo sapiens
brenda
Mihalik, S.J.; Rhead, W.J.
L-Pipecolic acid oxidation in the rabbit and cynomolgus monkey. Evidence for differing organellar locations and cofactor requirements in each species
J. Biol. Chem.
264
2509-2517
1989
Oryctolagus cuniculus, Macacine alphaherpesvirus 1
brenda
Kinzel, J.J.; Bhattacharjee, J.K.
Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase
J. Bacteriol.
151
1073-1077
1982
Rhodotorula glutinis
brenda
Yoshida, N.; Akazawa, S.I.; Katsuragi, T.; Tani, Y.
Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe
J. Biosci. Bioeng.
97
278-280
2004
Schizosaccharomyces pombe
brenda
Natarajan, S.K.; Muthukrishnan, E.; Khalimonchuk, O.; Mott, J.L.; Becker, D.F.
Evidence for pipecolate oxidase in mediating protection against hydrogen peroxide stress
J. Cell. Biochem.
118
1678-1688
2017
Homo sapiens, Homo sapiens (Q9P0Z9)
brenda
Posset, R.; Opp, S.; Struys, E.A.; Voelkl, A.; Mohr, H.; Hoffmann, G.F.; Koelker, S.; Sauer, S.W.; Okun, J.G.
Understanding cerebral L-lysine metabolism the role of L-pipecolate metabolism in Gcdh-deficient mice as a model for glutaric aciduria type I
J. Inherit. Metab. Dis.
38
265-272
2015
Mus musculus
brenda
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