This article is about a phosphatidylserine-specific phospholipase A1 encoded by PLA1A in humans. For the type of enzyme with broader activity, see phospholipase A1.
PLA1A
Identifiers
AliasesPLA1A, PS-PLA1, PSPLA1, phospholipase A1 member A
External IDsOMIM: 607460; MGI: 1934677; GeneCards: PLA1A
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
3.1.1.111↗↗↗↗
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

51365

85031

Ensembl

ENSG00000144837

ENSMUSG00000002847

UniProt

Q53H76

Q8VI78

RefSeq (mRNA)

NM_001206960
NM_001206961
NM_001293225
NM_015900

NM_134102

RefSeq (protein)

NP_001193889
NP_001193890
NP_001280154
NP_056984

NP_598863

Location (UCSC)n/aChr 16: 38.22 – 38.25 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Phospholipase A1 member A (EC 3.1.1.111) is an enzyme that in humans is encoded by the PLA1A gene. It acts as a phospholipase enzyme which removes the 1-acyl group, and is able to catalyze the following two reactions[4]

  • a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O ⇌ a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+)
  • a 1-acyl-sn-glycero-3-phospho-L-serine + H2O ⇌ sn-glycero-3-phospho-L-serine + a fatty acid + H(+)

Phospholipases are a type of enzyme that break down phospholipids, typically releasing fatty acids or other components.[5] They are typically separated into different classes according to the type of phospholipid bond they break. In particular, phospholipase A1 (PLA1) specifically catalyzes the cleavage at the sn-1 position of phospholipids, forming a fatty acid and a lysophospholipid.[6][7]

Phospholipase A1 cleaves phospholipid at the sn-1 position forming a lysophospholipid and a fatty acid.

Substrate specificity

Optimum pH conditions for PLA1 activity on neutral phospholipids is around 7.5, whereas the optimal conditions for PLA1 activity on acidic phospholipids is around 4.[8][9]

Structure

The structure of a PLA1 is a monomer that contains the following sequence: Gly-X-Ser-X-Gly, where X represents any other amino acid. The serine is considered the active site in the enzyme.[10] PLA1's also contain a catalytic triad of Ser-Asp-His, with a variety of cysteine residues needed for disulfide bond formation. The cysteine residues are responsible for key structural motifs such as the lid domain and the B9 domain, both of which are lipid binding surface loops. These two loops can vary between each PLA1. For example, a PLA1 enzyme with a long lid domain (22-23 amino acids) and a long B9 domain (18-19 amino acids) constitute an extracellular PLA1 exhibiting triacylglycerol hydrolase activity.[11] In contrast, a PLA1 enzyme that is considered more selective will have a short lid and B9 domain that span 7-12 and 12-13 amino acids, respectively.

Industrial use

Unlike other phospholipases such as PLA2, there is much that is unknown about PLA1 enzymes due to the difficulty of developing efficient ways to purify, clone, express, and characterize them.[11]

See also

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002847 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ EC 3.1.1.111
  5. ^ 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.
  6. ^ Richmond GS, Smith TK (2011). "Phospholipases A1". International Journal of Molecular Sciences. 12 (1): 588–612. doi:10.3390/ijms12010588. PMC 3039968. PMID 21340002.
  7. ^ 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.
  8. ^ Mebarek S, Abousalham A, Magne D, Do le D, Bandorowicz-Pikula J, Pikula S, Buchet R (2013). "Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations". International Journal of Molecular Sciences. 14 (3): 5036–129. doi:10.3390/ijms14035036. PMC 3634480. PMID 23455471.
  9. ^ Nishijima M, Akamatsu Y, Nojima S (Sep 1974). "Purification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei". J Biol Chem. 249 (17): 5658–67. doi:10.1016/S0021-9258(20)79778-4. PMID 4415399.
  10. ^ Aoki J, Inoue A, Makide K, Saiki N, Arai H (2007). "Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family". Biochimie. 89 (2): 197–204. doi:10.1016/j.biochi.2006.09.021. PMID 17101204.
  11. ^ a b Aoki J, Nagai Y, Hosono H, Inoue K, Arai H (May 2002). "Structure and function of phosphatidylserine-specific phospholipase A1". Biochim Biophys Acta. 1582 (1–3): 26–32. doi:10.1016/s1388-1981(02)00134-8. PMID 12069807.