DB code: S00148

CATH domain 2.60.120.200 : Jelly Rolls
E.C. 3.1.1.5
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.60.120.200 : Jelly Rolls D00535 D00666 M00185 S00511 T00064 T00208

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q05315 Eosinophil lysophospholipase
EC 3.1.1.5
Charcot-Leyden crystal protein
Lysolecithin acylhydrolase
CLC
Galectin-10
NP_001819.2 (Protein)
NM_001828.5 (DNA/RNA sequence)
PF00337 (Gal-bind_lectin)
[Graphical View]

KEGG enzyme name
lysophospholipase A1
lysophospholipase
lecithinase B
lysolecithinase
phospholipase B
lysophosphatidase
lecitholipase
phosphatidase B
lysophosphatidylcholine hydrolase
lysophopholipase L2
lysophospholipase transacylase
neuropathy target esterase
NTE
NTE-LysoPLA
NTE-lysophospholipase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q05315 LPPL_HUMAN 2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate. Cytoplasmic granule. Note=Localized in granules from where it may be secreted or transported to other locations in the cell.

KEGG Pathways
Map code Pathways E.C.
MAP00564 Glycerophospholipid metabolism

Compound table
Substrates Products Intermediates
KEGG-id C01174 C00001 C00670 C00060
E.C.
Compound 2-Lysophosphatidylcholine H2O Glycerophosphocholine Carboxylate
Type amine group,carbohydrate,lipid,phosphate group/phosphate ion H2O amine group,carbohydrate,phosphate group/phosphate ion carboxyl group
ChEBI 15377
 15377
PubChem 22247451
 962
 22247451
 962
 		439285
 58381695
 439285
 58381695
1lclA Unbound Unbound Unbound
1qkqA Unbound Unbound Unbound
1g86A Unbound Unbound Unbound
1hdkA Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1lclA
1qkqA
1g86A
1hdkA

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 6261258
Journal Proc Natl Acad Sci U S A
Year 1980
Volume 77
Pages 7440-3
Authors Weller PF, Goetzl EJ, Austen KF
Title Identification of human eosinophil lysophospholipase as the constituent of Charcot-Leyden crystals.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3936896
Journal J Lipid Res
Year 1985
Volume 26
Pages 1379-88
Authors Waite M
Title Approaches to the study of mammalian cellular phospholipases.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3221396
Journal J Mol Biol
Year 1988
Volume 204
Pages 489-91
Authors Sieker LC, Turley S, Le Trong I, Stenkamp RE, Weller PF, Ackerman SJ
Title Crystallographic characterization of human eosinophil Charcot-Leyden crystals.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID
PubMed ID 8747464
Journal Structure
Year 1995
Volume 3
Pages 1379-93
Authors Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR
Title Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
Related PDB 1lcl 1qkq
Related UniProtKB Q05315
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID
PubMed ID 10529229
Journal Biochemistry
Year 1999
Volume 38
Pages 13837-43
Authors Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR
Title Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution.
Related PDB
Related UniProtKB Q05315
[6]
Resource
Comments
Medline ID
PubMed ID 11834744
Journal J Biol Chem
Year 2002
Volume 277
Pages 14859-68
Authors Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR
Title Charcot-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 PDB 1g86 1hdk
Related UniProtKB

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.

Created Updated
2004-03-22 2009-02-26