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fosfolipaz

Fosfolipaz, also known as phospholipases, are a family of enzymes that catalyze the hydrolysis of phospholipids, the major components of cell membranes. They regulate membrane remodeling and lipid signaling, releasing fatty acids or generating lipid second messengers. Phospholipases are classified by the bond they cleave: A, C, and D types, with phospholipase B as a combined activity in some organisms. The A family includes A1 and A2; PLA1 removes the fatty acid at the sn-1 position of glycerophospholipids to form a lysophospholipid and a free fatty acid; PLA2 cleaves at the sn-2 position to yield a lysophospholipid and a free fatty acid, often liberating arachidonic acid as a precursor for eicosanoids. Phospholipase C enzymes cleave the glycerophosphodiester bond to produce diacylglycerol (DAG) and a phosphorylated head group, such as inositol trisphosphate (IP3). Phospholipase D enzymes split after the phosphate to form phosphatidic acid (PA) and an alcohol (for example choline). Phospholipase B combines A1 and A2 activities in some species and can fully hydrolyze the two fatty acyl chains.

Fosfolipaz exist as secreted and cytosolic forms in animals and as secreted toxins in bacteria and venom.

In
cellular
signaling,
PLC-derived
DAG
and
IP3
act
as
key
second
messengers
controlling
calcium
release
and
protein
kinase
activation;
PLA2
activity
provides
arachidonic
acid
for
inflammatory
mediators.
Dysregulation
of
phospholipases
is
linked
to
inflammatory
diseases,
pancreatitis,
and
neurodegenerative
conditions.
Industrial
and
research
applications
include
lipid
remodeling,
lipidomics
workflows,
and
the
modification
of
phospholipids
in
food,
pharmaceutical,
and
biotechnology
contexts.