Lipase

Lipases are a type of enzyme that break down fats. More specifically, lipases use water (as hydrolases) to remove fatty acids from fat molecules, especially triglycerides or its derivatives. In humans and other animals, lipases have a variety of roles in the body, from helping digest dietary fats like pancreatic lipase, to synthesizing fat-based hormones like diglyceride lipases.

What counts as a lipase is not consistently defined across sources, and some only consider enzymes to be lipases if they are activated by oil-water interfaces.

Many specific lipases can also catalyze other reactions. For example, carboxyl ester lipase is able to remove fatty acids that are attached to cholesterol, while endothelial lipase can remove fatty acids from phospholipids (a major component of cell membranes).

Structure and catalytic mechanism

Classically, lipases catalyse the hydrolysis of triglycerides:[citation needed] triglyceride + H 2 O ⟶ fatty acid + diacylglycerol diacylglycerol + H 2 O ⟶ fatty acid + monacylglycerol monacylglycerol + H 2 O ⟶ fatty acid + glycerol {\displaystyle {\begin{aligned}{\text{triglyceride}}+{\ce {H2O}}&\longrightarrow {\text{fatty acid}}+{\text{diacylglycerol}}\\[4pt]{\text{diacylglycerol}}+{\ce {H2O}}&\longrightarrow {\text{fatty acid}}+{\text{monacylglycerol}}\\[4pt]{\text{monacylglycerol}}+{\ce {H2O}}&\longrightarrow {\text{fatty acid}}+{\text{glycerol}}\end{aligned}}}

Lipases are serine hydrolases, i.e. they function by transesterification generating an acyl serine intermediate. Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3). For example, human pancreatic lipase (HPL), converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.

A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of protein folds and catalytic mechanisms. However, most are built on an alpha/beta hydrolase fold and employ a chymotrypsin-like hydrolysis mechanism using a catalytic triad consisting of a serine nucleophile, a histidine base, and an acid residue, usually aspartic acid.

Physiological distribution

Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling and inflammation. Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces.

• In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
• Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body.
• Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host).
• Certain wasp and bee venoms contain phospholipases that enhance the effects of injury and inflammation delivered by a sting.
• As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology.
• Malassezia globosa, a fungus thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff.

Genes encoding lipases are even present in certain viruses.

Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicansin human tissue.

Human lipases

Other traditional triglyceride lipases (EC) include Lipase member N, , , , and . In addition, there are various other non-traditional lipases including Monoacylglycerol lipases (eg: , ABHD2, and ABHD6), and Diacylglycerol lipases (eg: , , and ABHD11).

Not all lipase-family proteins function as lipases in humans. Some like Lipase member H and Lipase member I function as phospholipases, while others like pancreatic lipase related protein 1 (), , , and do not (yet) have a well established function as an enzyme.

Uses

In the commercial sphere, lipases are widely used in laundry detergents. Several thousand tons per year are produced for this role.

Lipases are catalysts for hydrolysis of esters and are useful outside of the cell, a testament to their wide substrate scope and ruggedness. The ester hydrolysis activity of lipases has been well evaluated for the conversion of triglycerides into biofuels or their precursors.

Lipases are chiral, which means that they can be used for the enantioselective hydrolysis prochiral diesters. Several procedures have been reported for applications in the synthesis of fine chemicals.

Lipases are generally animal sourced, but can also be sourced microbially.[citation needed]

Biomedicine

Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas. Measured serum lipase values may vary depending on the method of analysis.[citation needed]

In patients with exocrine pancreatic insufficiency, pancreatic enzyme replacement therapy (PERT) is used to replace the various enzymes that are produced by the pancreas the supplementation of pancreatic enzymes to treat. Enzyme mixtures used for PERT will include lipase, amylase, and protease.

See also

• Alpha toxin
• Pathology
• Lysosomal acid lipase deficiency
• Peripheral membrane proteins
• Phospholipase A
• Phospholipase C
• Triglyceride lipase
• Phospholipase A2
• Outer membrane phospholipase A1
• Patatin-like phospholipase

25. Gulzar, Bio-degradation of hydrocarbons using different bacterial and fungal species. Published in international conference on biotechnology and neurosciences. CUSAT (cochin university of science and technology), 2003

External links

• at the U.S. National Library of MedicineMedical Subject Headings(MeSH)