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Information on EC 3.1.1.5 - lysophospholipase and Organism(s) Kluyveromyces lactis and UniProt Accession O59863

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.5 lysophospholipase
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This record set is specific for:
Kluyveromyces lactis
UNIPROT: O59863 not found.
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Word Map
The taxonomic range for the selected organisms is: Kluyveromyces lactis
The enzyme appears in selected viruses and cellular organisms
Synonyms
phospholipase a, lysophospholipase, neuropathy target esterase, phospholipase b, lysopld, galectin-10, charcot-leyden crystal protein, lysophospholipase a, lysopl, cpla2gamma, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Charcot-Leyden crystal protein
-
-
-
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Charcot-Leyden crystal protein homolog
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-
-
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CLC
-
-
-
-
Galactin-10
-
-
-
-
Galectin-10
-
-
-
-
lecithinase B
-
-
-
-
lecitholipase
-
-
-
-
Lysolecithin acylhydrolase
-
-
-
-
lysolecithinase
-
-
-
-
lysophopholipase L2
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-
-
-
lysophosphatidase
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-
-
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lysophosphatidylcholine hydrolase
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-
-
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lysophospholipase A1
-
-
-
-
phosphatidase B
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-
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phospholipase B
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
2-lysophosphatidylcholine acylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-85-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
Ca2+, Fe3+ or Al3+ required
Ca2+
Ca2+, Fe3+ or Al3+ required
Fe3+
Ca2+, Fe3+ or Al3+ required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
and a second optimum at pH 7.5
7.5
and a second optimum at pH 2.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D406A
loss of enzymatic activity
R112A
loss of enzymatic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oishi, H.; Morimoto, T.; Watanabe, Y.; Tamai, Y.
Purification and characterization of phospholipase B from Kluyveromyces lactis, and cloning of phospholipase B gene
Biosci. Biotechnol. Biochem.
63
83-90
1999
Kluyveromyces lactis (O59863), Kluyveromyces lactis
Manually annotated by BRENDA team