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Human chitinases may explain the link between some of the most common allergies (dust mites, mold spores—both of which contain chitin) and worm infections, as part of one version of the hygiene hypothesis [31] [32] [33] (worms have chitinous mouthparts to hold the intestinal wall).
Chitinase-3-like protein 1 (CHI3L1), also known as YKL-40, is a secreted glycoprotein that is approximately 40kDa in size that in humans is encoded by the CHI3L1 gene. [ 5 ] [ 6 ] [ 7 ] The name YKL-40 is derived from the three N-terminal amino acids present on the secreted form and its molecular mass .
Chitinase domain-containing protein 1 (CHID1) is a highly conserved protein of unknown function located on the short (p) arm of chromosome 11 near the telomere. [5] The protein has 27 introns, which allows for many isoforms of this gene. It has several aliases, the most common of which is Stabilin-1 interacting chitinase-like protein (SI-CLP).
Chitinases [8] are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitinases belong to glycoside hydrolase families 18 or 19. [ 9 ] Chitinases of family 19 (also known as classes IA or I and IB or II) are enzymes from plants that function in the defence against fungal and insect ...
Hofmann hydrolyzed chitin using a crude preparation of the enzyme chitinase, which he obtained from the snail Helix pomatia. [ 7 ] [ 8 ] [ 9 ] Chitin is a modified polysaccharide that contains nitrogen; it is synthesized from units of N -acetyl- D -glucosamine (to be precise, 2-(acetylamino)-2-deoxy- D -glucose).
Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [ 13 ] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation ...
In this chitinase function, the enzyme contributes to the ability of many organisms to break down chitin-containing molecules and subsequently digest or re-uptake environmental chitin, carbon, or nitrogen. The enzyme's crystal structure varies slightly across organisms, but is characterized by three or four domains with one active site.
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.