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
3.3.2.2
-
RECOMMENDED NAME
GeneOntology No.
alkenylglycerophosphocholine hydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of ether bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ether lipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolase, alkenylglycerophosphocholine
-
-
-
-
lysoplasmalogenase
-
-
-
-
lysoplasmalogenase
-
lysoplasmalogenase
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
-
YhhN
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-65-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
overexpression in HEK 293T cells leads to decreased levels of plasmalogens
physiological function
the enzyme protects the bacterium from lysis by lysoplasmalogen derived from plasmalogens of the host
physiological function
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
the enzyme protects the bacterium from lysis by lysoplasmalogen derived from plasmalogens of the host
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
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
Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
show the reaction diagram
Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1
the enzyme catalyzes hydrolysis of the vinyl ether linkage at sn-1, is highly specific for the sn-2-deacylated (lyso) form of plasmalogen, and has no activity on the diradyl plasmalogens
-
?
lysoplasmenylcholine + H2O
an aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
additional information
?
-
-
no substrates are 1-(1-alkenyl)-2-acyl-sn-glycero-3-phosphocholine or 1-(1-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine
-
-
-
additional information
?
-
-
no substrate: 1-alkenyl-2-acyl-sn-glycero-3-phosphocholine or 1-alkenyl-2-acyl-sn-glycero-3-phosphoethanolamine, 1-acyl-sn-glycero-3-phosphocholine or 1-acyl-sn-glycero-3-phosphoethanolamine, and lysophosphatidic acid
-
-
-
additional information
?
-
Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1
the enzyme has no activity on diradyl plasmalogen, 1-alkenyl-glycerol, and monoacylglycerophospho-ethanolamine, ethanolamine plasmalogen, choline plasmalogen, monoacylglycerophospho-choline, lysophosphatidic acid, or monoacylglycerophospho-choline
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
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
Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1
Q5ZU17
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
show the reaction diagram
Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1
Q5ZU17
the enzyme catalyzes hydrolysis of the vinyl ether linkage at sn-1, is highly specific for the sn-2-deacylated (lyso) form of plasmalogen, and has no activity on the diradyl plasmalogens
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
enhancement of activity, no absolute requirement
Mg2+
-
enhancement of activity, no absolute requirement
Mg2+
75% residual activity at 10 mM
additional information
-
Ca2+, Mg2+ or Mn2+ do not affect the activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deoxycholate
-
3.2 mM, 50% inhibition
iodoacetate
-
12 mM, 17% inhibition
octyl glucoside
-
10 mM, 50% inhibition
p-chloromercuribenzoate
-
-
Phenylmethylsulfonylfluoride
-
6 mM 29% inhibition
Triton X-100
-
0.09 mM, 50% inhibition
lysophosphatidic acid
-
competitive
additional information
-
not inhibitory at 5 mM: Ca2+, Mg2+, Mn2+, EDTA, NaF or PMSF, phosphatidic acid, sphingosine 1-phosphate, monoacylglycerophosphocholine, and monoacylglycerophosphoethanolamine
-
additional information
not inhibited by EDTA, lysophosphatidic acid, sodium fluoride, phosphatidic acid, monoacylglycerophospho-choline, monoacylglycerophospho-ethanolamine, and phenylmethylsulfonyl fluoride
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
1-(1-alkenyl)-sn-glycero-3-phosphocholine
-
-
0.045
choline lysoplasmalogen
at pH 7.1, temperature not specified in the publication
-
0.045
ethanolamine lysoplasmalogen
at pH 7.1, temperature not specified in the publication
-
0.045
lysoplasmenylcholine
-
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.3
lysoplasmenylcholine
Rattus norvegicus
-
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
LITERATURE
IMAGE
10
octyl glucoside
-
-
0.09
Triton X-100
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
-
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
LITERATURE
6.6 - 7.1
-
substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
6.8 - 7.4
-
substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
7.2
-
substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
8.5
-
substrate 1-(1-alkenyl)-sn-glycero-3-phosphocholine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
at least 50% of maximum activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
-
3fold rise in activity from 25C to 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
87% of the activity
-
Manually annotated by BRENDA team
-
14% of the activity
Manually annotated by BRENDA team
additional information
-
not in cytosol
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 19000, SDS-PAGE
?
x * 18000, SDS-PAGE
?
Legionella pneumophila ATCC 33152D-5 Philadelphia-1
-
x * 18000, SDS-PAGE
-
additional information
-
enzyme is identical to protein Tmem86b, a hydrophobic transmembrane protein of the YhhN family
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41
-
inactivation above
137155
95
heating the enzyme to 95C for 3 min results in complete loss of activity
731362
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
-
-20C, stable in microsomes for several months, purified enzyme unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
native enzyme
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use in an assay system for phospholipase A2