Information on EC 3.3.2.2 - alkenylglycerophosphocholine hydrolase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.3.2.2
-
RECOMMENDED NAME
GeneOntology No.
alkenylglycerophosphocholine hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of ether bond
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ether lipid metabolism
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plasmalogen degradation
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SYSTEMATIC NAME
IUBMB Comments
1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-65-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
choline lysoplasmalogen + H2O
? + glycerophospho-choline
show the reaction diagram
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
show the reaction diagram
lysoplasmenylcholine + H2O
an aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
-
?
additional information
?
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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
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
choline lysoplasmalogen + H2O
? + glycerophospho-choline
show the reaction diagram
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
enhancement of activity, no absolute requirement
additional information
-
Ca2+, Mg2+ or Mn2+ do not affect the activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
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3.2 mM, 50% inhibition
iodoacetate
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12 mM, 17% inhibition
lysophosphatidic acid
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competitive
octyl glucoside
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10 mM, 50% inhibition
p-chloromercuribenzoate
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-
Phenylmethylsulfonylfluoride
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6 mM 29% inhibition
Triton X-100
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0.09 mM, 50% inhibition
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
1-(1-alkenyl)-sn-glycero-3-phosphocholine
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-
0.045
choline lysoplasmalogen
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.3
lysoplasmenylcholine
Rattus norvegicus
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pH 7.1, temperature not specified in the publication. Coupled enzyme assay, the aldehyde that is produced by hydrolysis of lysoplasmalogen is reduced to an alcohol in a second enzymic reaction. In the second reaction, NADH is oxidized in a 1:1 stoichiometry between the mol of aldehyde produced and mol of NADH oxidized
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
octyl glucoside
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0.09
Triton X-100
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.055
cell lysate, at pH 7.1, temperature not specified in the publication
8.443
after 153.5fold purification, at pH 7.1, temperature not specified in the publication
15.76
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pH 7.1, temperature not specified in the publication. Coupled enzyme assay, the aldehyde that is produced by hydrolysis of lysoplasmalogen is reduced to an alcohol in a second enzymic reaction. In the second reaction, NADH is oxidized in a 1:1 stoichiometry between the mol of aldehyde produced and mol of NADH oxidized
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 7.1
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substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
6.8 - 7.4
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substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
7.2
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substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
8.5
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substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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at least 50% of maximum activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
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3fold rise in activity from 25C to 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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not in cytosol
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme is identical to protein Tmem86b, a hydrophobic transmembrane protein of the YhhN family
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
-
inactivation above
95
heating the enzyme to 95C for 3 min results in complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
both un-tagged YhhN protein and the YhhN-GFP fusion require the continuous presence of 0.1% DDM (w/v) or 2-4 mM diradylglycerophospholipid for maintenance of activity at 4C. For storage at -20C, the presence of 50% (v/v) glycerol or 2-4 mM diradylglycerophospholipid is also required
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, stable for more than 12 months
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-20C, stable in microsomes for several months, purified enzyme unstable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme
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Ni-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43(DE3) cells as C-terminal-GFP-His8-fusion
functional expression both in Escherichia coli and HEK 293T cell
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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use in an assay system for phospholipase A2