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Information on EC 3.3.2.2 - lysoplasmalogenase
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3.3.2.2 lysoplasmalogenaseIUBMB Comments
Lysoplasmalogenase is specific for the sn-2-deacylated (lyso) form of plasmalogen and catalyses hydrolytic cleavage of the vinyl ether bond, releasing a fatty aldehyde and sn-glycero-3-phosphocholine or sn-glycero-3-phosphoethanolamine.
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
lysoplasmalogenase, tmem86b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
-
-
-
-
alkenylglycerophosphocholine hydrolase
-
-
-
-
EC 3.3.2.5
-
-
formerly
-
hydrolase, alkenylglycerophosphocholine
-
-
-
-
hydrolase, alkenylglycerophosphoethanolamine
-
-
-
-
lysoplasmalogenase
YhhN
lysoplasmalogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine
(1)
-
-
-
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = an aldehyde + sn-glycero-3-phosphoethanolamine
(2)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of ether bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
lysoplasmalogen aldehydohydrolase
Lysoplasmalogenase is specific for the sn-2-deacylated (lyso) form of plasmalogen and catalyses hydrolytic cleavage of the vinyl ether bond, releasing a fatty aldehyde and sn-glycero-3-phosphocholine or sn-glycero-3-phosphoethanolamine.
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CAS REGISTRY NUMBER
COMMENTARY
37288-65-6
-
78413-08-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
lysoplasmenylcholine + H2O
an aldehyde + sn-glycero-3-phosphocholine
-
-
-
-
?
lysoplasmenylethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
choline lysoplasmalogen + H2O
? + glycerophospho-choline
-
-
-
?
choline lysoplasmalogen + H2O
? + glycerophospho-choline
-
-
-
?
choline lysoplasmalogen + H2O
? + glycerophospho-choline
preferred substrate
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
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
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
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
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
6.5% of the activity with choline lysoplasmalogen
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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
?
-
no substrates: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, sphingomyelin, choline plasmalogen, ethanolamine plasmalogen
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O
aldehyde + sn-glycero-3-phosphocholine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O
aldehyde + sn-glycero-3-phosphoethanolamine
-
-
-
?
choline lysoplasmalogen + H2O
? + glycerophospho-choline
-
-
-
?
choline lysoplasmalogen + H2O
? + glycerophospho-choline
-
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
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
-
-
?
ethanolamine lysoplasmalogen + H2O
? + glycerophospho-ethanolamine
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibited by EDTA, lysophosphatidic acid, sodium fluoride, phosphatidic acid, monoacylglycerophospho-choline, monoacylglycerophospho-ethanolamine, and phenylmethylsulfonyl fluoride
-
additional information
-
not inhibited by EDTA, lysophosphatidic acid, sodium fluoride, phosphatidic acid, monoacylglycerophospho-choline, monoacylglycerophospho-ethanolamine, and phenylmethylsulfonyl fluoride
-
additional information
-
not inhibitory at 5 mM: Ca2+, Mg2+, Mn2+, EDTA, NaF or PMSF, phosphatidic acid, sphingosine 1-phosphate, monoacylglycerophosphocholine, and monoacylglycerophosphoethanolamine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.053
lysoplasmenylethanolamine
-
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
0.045
choline lysoplasmalogen
at pH 7.1, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.3
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
10.3
lysoplasmenylethanolamine
-
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.055
cell lysate, 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
8.443
after 153.5fold purification, at pH 7.1, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 7.1
6.8 - 7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
-
the enzyme protects the bacterium from lysis by lysoplasmalogen derived from plasmalogens of the host
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TM86B_BOVIN
224
6
24681
Swiss-Prot
Secretory Pathway (Reliability: 5)
TM86B_HUMAN
226
6
24352
Swiss-Prot
Secretory Pathway (Reliability: 5)
TM86B_MOUSE
226
6
24989
Swiss-Prot
other Location (Reliability: 5)
TM86B_PIG
226
4
24489
Swiss-Prot
Secretory Pathway (Reliability: 5)
TM86B_RAT
233
6
25912
Swiss-Prot
Secretory Pathway (Reliability: 3)
LYPGN_LEGPH
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
216
7
24536
Swiss-Prot
-
LYPGN_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
261
8
27391
Swiss-Prot
-
LYPGN_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
261
8
27391
Swiss-Prot
-
LYPGN_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
261
8
27391
Swiss-Prot
-
B0BMQ4_XENTR
245
8
27768
TrEMBL
other Location (Reliability: 5)
A0A061HVY3_CRIGR
126
3
13917
TrEMBL
Secretory Pathway (Reliability: 1)
Q9VAJ0_DROME
254
8
28582
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0B4K6T8_DROME
142
3
15872
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is identical to protein Tmem86b, a hydrophobic transmembrane protein of the YhhN family
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A55D
47% of wild-type activity with substrate choline lysoplasmalogen
A55N
51.6% of wild-type activity with substrate choline lysoplasmalogen
F211A
20.0% of wild-type activity with substrate choline lysoplasmalogen
N56D
8.4% of wild-type activity with substrate choline lysoplasmalogen
N56Q
55.2% of wild-type activity with substrate choline lysoplasmalogen
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95
heating the enzyme to 95°C for 3 min results in complete loss of activity
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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 4°C. For storage at -20°C, the presence of 50% (v/v) glycerol or 2-4 mM diradylglycerophospholipid is also required
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43(DE3) cells as C-terminal-GFP-His8-fusion
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirashima, Y.; Jurkowitz-Alexander, M.S.; Farooqui, A.A.; Horrocks, L.A.
Continuous spectrophotometric assay of phospholipase A2 activity hydrolyzing plasmalogens using coupling enzymes
Anal. Biochem.
176
180-184
1989
Rattus norvegicus
brenda
Arthur, G.; Page, L.; Mock, T.; Choy, P.C.
The catabolism of plasmenylcholine in the guinea pig heart
Biochem. J.
236
475-480
1986
Cavia porcellus
brenda
Warner, H.R.; Lands, W.E.M.
The metabolism of plasmalogen: enzymatic hydrolysis of the vinyl ether
J. Biol. Chem.
236
2404-2409
1961
Rattus norvegicus
brenda
Jurkowitz, M.S.; Horrocks, L.A.; Litsky, M.L.
dentification and characterization of alkenyl hydrolase (lysoplasmalogenase) in microsomes and identification of a plasmalogen-active phospholipase A2 in cytosol of small intestinal epithelium
Biochim. Biophys. Acta
1437
142-156
1999
Rattus norvegicus
brenda
Jurkowitz-Alexander, M.; Ebata, H.; Mills, J.S.; Murphy, E.J.; Horrocks, L.A.
Solubilization, purification and characterization of lysoplasmalogen alkenylhydrolase (lysoplasmalogenase) from rat liver microsomes
Biochim. Biophys. Acta
1002
203-212
1989
Rattus norvegicus
brenda
Hirashima, Y.; Farooqui, A.A.; Horrocks, L.A.
Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver
Biochem. J.
260
605-608
1989
Rattus norvegicus
brenda
Hirashima, Y.; Farooqui, A.A.; Horrocks, L.A.
Assay procedures and properties of plasmalogenase, lysoplasmalogenase and plasmalogen specific phospholipase A2
Front. Chem.
1
91-102
1989
Rattus norvegicus
-
brenda
Gunawan, J.; Debuch, H.
Liberation of free aldehyde from 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) by rat liver microsomes
Hoppe-Seyler's Z. Physiol. Chem.
362
445-452
1981
Rattus norvegicus
brenda
Gunawan, J.; Debuch, H.
Lysoplasmalogenase - a microsomal enzyme from rat brain
J. Neurochem.
39
693-699
1982
Rattus norvegicus
brenda
Wu, L.C.; Pfeiffer, D.R.; Calhoon, E.A.; Madiai, F.; Marcucci, G.; Liu, S.; Jurkowitz, M.S.
Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen
J. Biol. Chem.
286
24916-24930
2011
Rattus norvegicus
brenda
Jurkowitz, M.S.; Patel, A.; Wu, L.C.; Krautwater, A.; Pfeiffer, D.R.; Bell, C.E.
The YhhN protein of Legionella pneumophila is a lysoplasmalogenase
Biochim. Biophys. Acta
1848
742-751
2015
Legionella pneumophila (Q5ZU17), Legionella pneumophila, Legionella pneumophila ATCC 33152D-5 Philadelphia-1 (Q5ZU17)
brenda
Matsumoto, Y.; Kashiwabara, N.; Oyama, T.; Murayama, K.; Matsumoto, H.; Sakasegawa, S.; Sugimori, D.
Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D from Thermocrispum sp.
FEBS Open Bio
6
1113-1130
2016
Thermocrispum sp. RD004668 (A0A0U4VTN7)
brenda
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