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A Review on L-Asparaginase
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Chitinase has antimicrobial activity. The chitin, which is present in the cell wall of most pathogenic organisms like fungi, protozoa and helminths, is a good target for antimicrobials (Fusetti et al., 2002). The lytic enzymes derived from bacteriophages can be utilized for the treatment of several infections. They also exhibit activity against new resistant bacterial species. Proteolytic enzymes isolated from bacterial sources have anti-inflammatory properties. These proteolytic enzymes are also employed to eliminate burned skin (Gurung et al., 2013).
Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Chitin and chitooligosaccharides had hypolipidemic effects, lowering LDL cholesterol and TG concentration in blood, and angiotensin I–converting enzyme (ACE) inhibitor had antihypertensive efficacy. Furthermore, chitin promotes wound healing by boosting macrophage formation and cytokine release. Chitinase is an antifungal agent that can be taken in association with antifungal medicines to treat fungal infections. Enzymes are increasingly being used in various aspects of the food industry, and chitinases offer a wide variety of applications in this area. Because of their antibacterial properties, chitin compounds prevent the proliferation of spoilage bacteria in foods, inhibiting food contamination. In agriculture, chitinases are fascinating enzymes. The chitinous recycling of the waste into biofertilizers is the most notable aspect. Pollution of agricultural soil with fungal infections might render it unprofitable at times. Using large-scale biopesticides to manage fungal infections and pests is one option, but it comes at a high cost. Biological control is an effective technique to mitigate such issues. Chitinases are used to treat a variety of illnesses, including pathogenic fungi, viral diseases, and insect pests, as antifungal, insecticidal, or antiparasitic medicines.
Translational Research
Published in Goh Cheng Soon, Gerard Bodeker, Kishan Kariippanon, Healthy Ageing in Asia, 2022
BLAST analysis of the N-terminal sequence of DOI disclosed an elevated E-value exceeding 10−3, showing its novelty. DOI belongs to the chitinase-like superfamily. BLAST analysis of the partial amino acid sequence of DOI revealed its pronounced resemblance to the 27.9-kDa Dioscorea japonica chitinase (AAB23692.1) and the 31.4-kDa Dioscorea oppositifolia chitinase (BAC56863.1). Mass spectrometry analysis of DOI tryptic peptides revealed ten peptides that matched peptides in Dioscorea japonica acidic endochitinase. The identified peptides are highlighted in bold in the partial sequence of acidic endochitinase. The N-terminal sequence manifested dissimilarities from the 31.4-kDa Dioscorea oppositifolia chitinase (BAC56863.1). DOI did not exhibit any discernible chitinase activity toward different chitinase substrates, including 4-nitrophenyl N-acetyl-β-D-glucosaminide, 4-nitrophenyl N,N′-diacetyl-β-D-chitobioside, and 4-nitrophenyl β-D-N,N′,N′′-triacetylchitotriose (N8638).
A genetic variation in CHI3L1 is associated with bronchial asthma
Published in Archives of Physiology and Biochemistry, 2021
Jinlian Shao, Xuexi Yang, Dunqiang Ren, Yaling Luo, Wenyan Lai
Chitinases are a family of evolutionarily conserved hydrolases characterized by their ability to cleave chitin. In addition to true chitinases, chitinase-like proteins have a chitin-binding ability but lack enzymatic activity. Both chitinases and chitinase-like proteins are potent up-regulators or down-regulators of the innate immune response (Hakala et al. 1993, Ober et al. 2008). Chitinase 3-like 1 (CHI3L1), also known as YKL-40 or human cartilage glycoprotein 39 (HCgp-39), is a 40-kD mammalian glycoprotein. The CHI3L1 gene is located on chromosome 1q32.1. Prominent expression of YKL-40 has been associated with pathologic conditions characterized by tissue inflammation and remodeling, or by aberrant cell growth, such as atherosclerosis, schizophrenia, liver fibrosis and several malignancies (Boot et al. 1999, Johansen et al. 2000, 2006, Rathcke et al. 2006, Kim et al. 2007, Kucur et al. 2007). A recent study reported that plasma YKL-40 levels were elevated in patients with asthma (Chupp et al. 2007).
Structure-based virtual screening of highly potent inhibitors of the nematode chitinase CeCht1
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Wei Chen, Qi Chen, Ashutosh Kumar, Xi Jiang, Kam Y. J. Zhang, Qing Yang
The scarce nematode chitinase inhibitors may be, to a great extent, attributed to the lagged research on the structure of nematode chitinases. The availability of structure information could facilitate both structure-based virtual screening for inhibitor development and elucidation of inhibitory mechanism for inhibitor optimization24–27. Recently, we resolved the crystal structure of CeCht1 (PDB ID: 6LDU), a chitinase from the model nematode C. elegans28. In this study, exploiting the structure of CeCht1, we identified a series of inhibitors bearing a (R)-3,4-diphenyl-4,5-dihydropyrrolo[3,4-c]pyrazol-6(2H)-one (PP) scaffold. In addition, we demonstrated the binding mechanism by X-ray crystallographic analysis, which facilitated the further optimisation of these compounds and led to the identification of several compounds with improved inhibitory activity. This work provides a solid basis for the development of nematode chitinase inhibitors.
Serum chitotriosidase: a circulating biomarker in polycythemia vera
Published in Hematology, 2018
Ivan Krecak, Velka Gveric-Krecak, Pavle Roncevic, Sandra Basic-Kinda, Josipa Gulin, Ivana Lapic, Ksenija Fumic, Ivana Ilic, Ivana Horvat, Renata Zadro, Hrvoje Holik, Bozena Coha, Nena Peran, Igor Aurer, Nadira Durakovic
Chitotriosidase enzyme (CHIT1 or chitinase-1), belongs to a family of various chitinase and chitinase-like proteins, and is one of the most abundantly secreted proteins, being mainly produced by activated macrophages, granulocytes and epithelial cells. Its natural substrate chitin is the second most abundant polysaccharide in nature after cellulose. Chitin is a polymer of N-acetylglucosamine and the main component of the cell walls of fungi and protozoa, egg shells of helminthes, and the exoskeletons of arthropods and insects. Although mammals do not contain chitin, CHIT1 plays a pivotal role in the defense against chitin-containing microorganisms such as fungi, insects and some bacteria [31–37]. Macrophages release CHIT1 after toll-like receptor stimulation and after stimulation with lipopolysaccharide, granulocyte-macrophage colony-stimulating factor (GM-CSF), interferon-gamma and TNF-α [38,39].