Question

.What is the mechanism of the lipase? How do you think the enzyme specifies the cleavage of the C-1 and C-3 fatty acids from TAG? (hydrophobic, stearic, hydrophilic or ... )

Answer 1

Answer:

Mechanism of lipase:

• Lipase enzymes catalyze the hydrolysis of the ester bonds in fats (triglycerides).
• The active site of lipase consists of a catalytic traid of Ser-His-Asp/Glu. Serine acts as a nucleophile, histidine acts as a base and Asparatic or Glutamic acid forms the acidic residue.
• The mechanism of lipase action (transacylation) involves the serine nucleophile to attack the ester carbonyl group on the fatty acids. It can be one of the fatty acids present on the 1 or 3 carbon of the glycerol backbone.

Enzymes specifies the cleavage of the C1 and C3 fatty acids from TAG?

1,3-specific lipases only hydrolyse triacylglycerols at the C1 and C3 carbon (primary ester bonds) of the glycerol bonds. Hydrolysis by lipase yields fatty acids, monoacylglycerols and or diacylglycerols. Lipase contains distinct distribution of hydrophobic and hydrophilic residues.This selective hydrolysis is performed in a hydrophobic environment.