EzCatDB: S00148
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DB codeS00148
CATH domainDomain 12.60.120.200 : Jelly Rolls
E.C.3.1.1.5

CATH domainRelated DB codes (homologues)
2.60.120.200 : Jelly RollsD00535,D00666,M00185,S00511,T00064,T00208

Enzyme Name
UniProtKBKEGG

Q05315
Protein nameEosinophil lysophospholipaselysophospholipase
lecithinase B
lysolecithinase
phospholipase B
lysophosphatidase
lecitholipase
phosphatidase B
lysophosphatidylcholine hydrolase
lysophospholipase A1
lysophopholipase L2
lysophospholipase transacylase
neuropathy target esterase
NTE
NTE-LysoPLA
NTE-lysophospholipase
SynonymsEC 3.1.1.5
Charcot-Leyden crystal protein
Lysolecithin acylhydrolase
CLC
Galectin-10
RefSeqNP_001819.2 (Protein)
NM_001828.5 (DNA/RNA sequence)
PfamPF00337 (Gal-bind_lectin)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00564Glycerophospholipid metabolism

UniProtKB:Accession NumberQ05315
Entry nameLPPL_HUMAN
Activity2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate.
Subunit
Subcellular locationCytoplasmic granule. Note=Localized in granules from where it may be secreted or transported to other locations in the cell.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01174C00001C00670C00060
Compound2-LysophosphatidylcholineH2OGlycerophosphocholineCarboxylate
Typeamine group,carbohydrate,lipid,phosphate group/phosphate ionH2Oamine group,carbohydrate,phosphate group/phosphate ioncarboxyl group
ChEBI
15377


PubChem
962
22247451
58381695
439285

            
1lclAUnbound UnboundUnbound
1qkqAUnbound UnboundUnbound
1g86AUnbound UnboundUnbound
1hdkAUnbound UnboundUnbound

Active-site residues
pdb
        
1lclA
1qkqA
1g86A
1hdkA


references
[1]
PubMed ID6261258
JournalProc Natl Acad Sci U S A
Year1980
Volume77
Pages7440-3
AuthorsWeller PF, Goetzl EJ, Austen KF
TitleIdentification of human eosinophil lysophospholipase as the constituent of Charcot-Leyden crystals.
[2]
PubMed ID3936896
JournalJ Lipid Res
Year1985
Volume26
Pages1379-88
AuthorsWaite M
TitleApproaches to the study of mammalian cellular phospholipases.
[3]
PubMed ID3221396
JournalJ Mol Biol
Year1988
Volume204
Pages489-91
AuthorsSieker LC, Turley S, Le Trong I, Stenkamp RE, Weller PF, Ackerman SJ
TitleCrystallographic characterization of human eosinophil Charcot-Leyden crystals.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
PubMed ID8747464
JournalStructure
Year1995
Volume3
Pages1379-93
AuthorsLeonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR
TitleCrystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
Related PDB1lcl,1qkq
Related UniProtKBQ05315
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
PubMed ID10529229
JournalBiochemistry
Year1999
Volume38
Pages13837-43
AuthorsSwaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR
TitleSelective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution.
Related UniProtKBQ05315
[6]
PubMed ID11834744
JournalJ Biol Chem
Year2002
Volume277
Pages14859-68
AuthorsAckerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR
TitleCharcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion.
Related PDB1g86,1hdk

comments
According to the literature [5] & [6], this protein was thought to have lysophospholipase activity before, but turned out to be not an enzyme. However, it binds a lysophospholipase inhibitor as well as with lisophospholipase itself (see [6]). It awaits some more information on this protein.

createdupdated
2004-03-222009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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