Lysophospholipase

Last updated
lysophospholipase
Identifiers
EC no. 3.1.1.5
CAS no. 9001-85-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins
Lysophospholipase, catalytic region
Identifiers
SymbolPLA2_B
Pfam PF01735
InterPro IPR002642
SMART SM00022
PROSITE PDOC51210
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB PDB: 1cjy

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

Contents

2-lysophosphatidylcholine + H2O glycerophosphocholine + a carboxylate

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B (EC 3.1.1.5) and cytosolic phospholipase A2 which also has a C2 domain InterPro :  IPR000008 . Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells. [1] Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, [2] the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in. [2]

The systematic name of this enzyme class is 2-lysophosphatidylcholine acylhydrolase. Other names in common use include lecithinase B, lysolecithinase, phospholipase B, lysophosphatidase, lecitholipase, phosphatidase B, lysophosphatidylcholine hydrolase, lysophospholipase A1, lysophopholipase L2, lysophospholipase transacylase, neuropathy target esterase, NTE, NTE-LysoPLA, and NTE-lysophospholipase. This enzyme participates in glycerophospholipid metabolism.

Examples

Human genes encoding proteins that contain this domain include:

See also

Related Research Articles

Phosphatidic acids are anionic phospholipids important to cell signaling and direct activation of lipid-gated ion channels. Hydrolysis of phosphatidic acid gives rise to one molecule each of glycerol and phosphoric acid and two molecules of fatty acids. They constitute about 0.25% of phospholipids in the bilayer.

<span class="mw-page-title-main">Monoacylglycerol lipase</span> Class of enzymes

Monoacylglycerol lipase is an enzyme that, in humans, is encoded by the MGLL gene. MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239.

<span class="mw-page-title-main">Phosphorylase kinase</span>

Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase “a” form over the less active glycogen phosphorylase b.

<span class="mw-page-title-main">Phospholipase A1</span>

Phospholipase A1 (EC 3.1.1.32; systematic name: phosphatidylcholine 1-acylhydrolase) encoded by the PLA1A gene is a phospholipase enzyme which removes the 1-acyl group:

<span class="mw-page-title-main">Bile salt-dependent lipase</span> Mammalian protein found in Homo sapiens

Bile salt-dependent lipase, also known as carboxyl ester lipase is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic secretions of all species in which it has been looked for. BSSL, originally discovered in the milk of humans and various other primates, has since been found in the milk of many animals including dogs, cats, rats, and rabbits.

<span class="mw-page-title-main">ARF1</span> Protein-coding gene in the species Homo sapiens

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.

<span class="mw-page-title-main">Leukotriene-A4 hydrolase</span>

Leukotriene A4 hydrolase, also known as LTA4H is a human gene. The protein encoded by this gene is a bifunctional enzyme which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.

<span class="mw-page-title-main">Acyloxyacyl hydrolase</span> Protein family

The enzyme acyloxyacyl hydrolase (EC 3.1.1.77, AOAH) was discovered because it catalyzes the reaction

<span class="mw-page-title-main">Protein-glutamate methylesterase</span>

The enzyme protein-glutamate methylesterase (EC 3.1.1.61) catalyzes the reaction

<span class="mw-page-title-main">PLA2G2A</span> Protein-coding gene in the species Homo sapiens

Phospholipase A2, membrane associated is an enzyme that in humans is encoded by the PLA2G2A gene.

In enzymology, a myosin-heavy-chain kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Carboxylesterase 1</span> Protein-coding gene in the species Homo sapiens

Liver carboxylesterase 1 also known as carboxylesterase 1 is an enzyme that in humans is encoded by the CES1 gene. The protein is also historically known as serine esterase 1 (SES1), monocyte esterase and cholesterol ester hydrolase (CEH). Three transcript variants encoding three different isoforms have been found for this gene. The various protein products from isoform a, b and c range in size from 568, 567 and 566 amino acids long, respectively.

<span class="mw-page-title-main">PLCB2</span> Protein-coding gene in the species Homo sapiens

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme that in humans is encoded by the PLCB2 gene.

<span class="mw-page-title-main">CAMK1</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.

<span class="mw-page-title-main">ARF3</span> Protein-coding gene in the species Homo sapiens

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.

<span class="mw-page-title-main">PHKG1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.

<span class="mw-page-title-main">ATP6V0D1</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.

<span class="mw-page-title-main">AADAC</span> Protein-coding gene in the species Homo sapiens

Arylacetamide deacetylase is an enzyme that in humans is encoded by the AADAC gene.

<span class="mw-page-title-main">Neuropathy target esterase</span> Protein-coding gene in the species Homo sapiens

Neuropathy target esterase, also known as patatin-like phospholipase domain-containing protein 6 (PNPLA6), is an esterase enzyme that in humans is encoded by the PNPLA6 gene.

<span class="mw-page-title-main">1-Lysophosphatidylcholine</span>

2-acyl-sn-glycero-3-phosphocholines are a class of phospholipids that are intermediates in the metabolism of lipids. Because they result from the hydrolysis of an acyl group from the sn-1 position of phosphatidylcholine, they are also called 1-lysophosphatidylcholine. The synthesis of phosphatidylcholines with specific fatty acids occurs through the synthesis of 1-lysoPC. The formation of various other lipids generates 1-lysoPC as a by-product.

References

  1. Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca2+-dependent lipid-binding domain and a Ca2+-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. doi: 10.1016/S0021-9258(17)32440-7 . PMID   8027085.
  2. 1 2 Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. doi: 10.1016/S0021-9258(17)32081-1 . PMID   8051052.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR002642