Phospholipase A1

Crystallographic structure of phospholipase A1. Red region denotes α helices, Green region denotes loops, and yellow region denotes β sheets.
Identifiers
EC no.3.1.1.32
CAS no.9043-29-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
phospholipase A1 member A
Identifiers
SymbolPLA1A
NCBI gene51365
HGNC17661
OMIM607460
RefSeqNM_015900
UniProtQ53H76
Other data
EC number3.1.1.32
LocusChr. 3 q13.13-13.2
Search for
StructuresSwiss-model
DomainsInterPro

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:[1]

phosphatidylcholine + H2O ⇌ 2-acylglycerophosphocholine + a carboxylate

It is an enzyme that resides in a class of enzymes called phospholipase that hydrolyze phospholipids into fatty acids.[2] There are four classes, separated according to the type of reaction they catalyze. In particular, phospholipase A1 (PLA1) specifically catalyzes the cleavage at the sn-1 position of phospholipids, forming a fatty acid and a lysophospholipid.[3][4]

Phospholipase A1 cleaves phospholipid at the sn-1 position forming a lysophospholipid and a fatty acid.
  1. ^ Phospholipase+A1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  2. ^ DeSilva NS, Quinn PA (1999). "Characterization of phospholipase A1, A2, C activity in Ureaplasma urealyticum membranes". Mol. Cell. Biochem. 201 (1–2): 159–67. doi:10.1023/A:1007082507407. PMID 10630635. S2CID 22101516.
  3. ^ Richmond GS, Smith TK (2011). "Phospholipases A1". International Journal of Molecular Sciences. 12 (1): 588–612. doi:10.3390/ijms12010588. PMC 3039968. PMID 21340002.
  4. ^ Scandella CJ, Kornberg A (November 1971). "A membrane-bound phospholipase A1 purified from Escherichia coli". Biochemistry. 10 (24): 4447–56. doi:10.1021/bi00800a015. PMID 4946924.