Chitinase [SEP] found in taxon
assumed that chitin digestion by animals requires bacterial symbionts and lengthy fermentations, similar to cellulase digestion by ruminants. Nevertheless, chitinases have been isolated from the stomachs of certain mammals, including humans.
Chitinase activity can also be detected in human blood and possibly cartilage. As in plant chitinases this may be related to pathogen resistance.
Clinical significance.
Chitinases produced in the human body (known as "human chitinases") may be related in response to allergies, and asthma has been linked to enhanced chitinase expression levels.
Chitinase A N-terminal domain
In molecular biology, the chitinase A N-terminal domain is found at the N-terminus of a number of bacterial chitinases and similar viral proteins. It is organised into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin. It is separated by a hinge region from the catalytic domain; this hinge region is probably mobile, allowing the N-terminal domain to