Information on EC 1.5.3.7 - L-pipecolate oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.3.7
-
RECOMMENDED NAME
GeneOntology No.
L-pipecolate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation II (L-pipecolate pathway)
-
-
L-lysine degradation V
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-pipecolate:oxygen 1,6-oxidoreductase
The product reacts with water to form (S)-2-amino-6-oxohexanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
81669-65-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cynomolgus monkey
-
-
Manually annotated by BRENDA team
strains Wis 54-1255, HS1-, and 10.25
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
strains wild-type, MU-1 and lys5
-
-
Manually annotated by BRENDA team
gene FAP1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-1,3-thiazane-4-carboxylic acid + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
show the reaction diagram
L-proline + O2
?
show the reaction diagram
-
low activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-pipecolate + O2
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
show the reaction diagram
additional information
?
-
-
enzyme is involved in L-lysine metabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-1,3-thiazane-4-carboxylic acid
-
causes time-dependent, irreversible, stereospecific inactivation
antimycin A
HgCl2
-
100% inhibition at 1 mM
hydroxylamine
-
15% inhibition at 1 mM
KCN
-
20% inhibition at 1 mM
L-homocysteine
-
at 0.005 mM 12% inactivation after 1 h incubation
L-proline
p-chloromercuribenzoate
-
100% inhibition at 1 mM
phenazine ethosulfate
-
-
rotenone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
di-(2-ethylhexyl)phthalate
-
5 g per kg body weight, 500% activity enhancement in the peroxisomal fraction
glucagon
-
3 mg per kg body weight, 150% activity enhancement in the mitochondrial fraction
additional information
-
activity is maximal when FAD, phenazine ethosulfate and glycerol are included in the assay
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.07
L-pipecolate
-
pH 8.0, 30C, recombinant enzyme
0.74 - 6
L-Pipecolic acid
3 - 3.5
L-proline
-
pH 8.0, 30C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36
(S)-1,3-thiazane-4-carboxylic acid
-
competitive inhibitor that completely inactivates the enzyme
10 - 11
L-proline
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
strain Wis 54-1255, HS1-, 10.25
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
1 * 43000, SDS-PAGE
46000
-
1 * 46000, SDS-PAGE
56000
-
2 * 56000, about, recombinant enzyme, SDS-PAGE
98000
-
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 56000, about, recombinant enzyme, SDS-PAGE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
10 min 20% activity, bovine serum albumin at 1 mg per ml protects from thermal inactivation
53
-
complete inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, Tris-HCl buffer pH 8.7, 1 mM 2-mercaptoethanol, several weeks, 100% activity
-
4C, Tris-HCl buffer pH 8.7, 1 mM 2-mercaptoethanol, several days, 100% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain JM109
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
-
expressed as a chimera between maltose-binding protein and L-pipecolic acid oxidase; expressed in Escherichia coli BL21
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expressed in Escherichia coli DH10B
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine