Elastase

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins, specifically one that can break down elastin. In other words, the name generally refers to the substrate specificity (i.e. what proteins it can digest), not to any kind of evolutionary grouping. However, this definition is not always used consistently, and some related proteases like CELA3A and CELA3B, which mostly do not have the ability to break down elastin, have historically been called elastases.

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins, specifically one that can break down elastin. In other words, the name generally refers to the substrate specificity (i.e. what proteins it can digest), not to any kind of evolutionary grouping. However, this definition is not always used consistently, and some related proteases like CELA3A and CELA3B, which mostly do not have the ability to break down elastin, have historically been called elastases. ==Forms and classification== Eight human genes encode elastases or are part of the classical elastase family (*) Though CELA3A/CELA3B are often referred to as elastases, they have little to no ability to actually break down elastin, and are instead sometimes referred to as "pancreatic endopeptidase E". The five chymotrypsin-like elastases, chymotrypsin-C, and neutrophil elastase are all serine proteases. The "macrophage elastase" is a matrix metallopeptidase. Chymotrypsin-C is less able breaking down elastin than pancreatic elastases like CELA2A and CELA2B. Some bacteria (including Pseudomonas aeruginosa) also produce elastase; bacterial elastases work in many ways and include serine proteases, aspartic proteases, thiol proteases, and metalloenzymes. ==References== ==External links== GeneReviews/NCBI/NIH/UW entry on ELANE-Related Neutropenias including cyclic neutropenia

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