Taxonomic group: fungi / Ascomycota, Ascomycota, Ascomycota, Basidiomycota
(Phylum: Ascomycota, Ascomycota, Ascomycota, Basidiomycota)
Organ / tissue: cell wallAssociated disease: infection due to Aspergillus fumigatus [ICD11:
XN5Z7 
];
infection due to Cryptococcus neoformans [ICD11:
XN3EH 
]
Publication DOI: 10.1080/mmy.39.1.55.66Journal NLM ID: 9815835Publisher: Oxford: Oxford University Press
Correspondence: cameron_douglas

merck.com
Institutions: Department of Human and Animal Infectious Diseases, Merck & Co., Rahway, New Jersey 07065, USA
The polysaccharide β(1,3)-D-glucan is a component of the cell wall of many fungi. Synthesis of the linear polymer is catalysed by UDP-glucose β(1,3)-D-glucan β(3)-D-glucosyltransferase. Because this enzyme has a key role in fungal cell-wall synthesis, and because many organisms that are responsible for human mycoses, including Candida albicans, Aspergillus fumigatus and Cryptococcus neoformans, produce walls that are rich in β(1,3)-glucan, it has been and remains the focus of intensive study. From early characterization of the enzymatic activity in Saccharomyces cerevisiae, advances have been made in purification of the enzyme, identification of essential subunits and description of regulatory circuitry that controls expression and localization of different components of the multisubunit enzyme complex. Progress in each of these areas has been enhanced dramatically by the availability of specific inhibitors of the enzymatic reaction that produces β(1,3)-glucan. These natural product inhibitors have utility both as tools to dissect the biology of β(1,3)-glucan synthase and as sources for development of semisynthetic derivatives with clinical utility in treatment of human fungal disease. This review will focus on the biochemistry, genetics and regulation of the enzyme.
β(1, 3)-glucan, FKS genes, echinocandin
Structure type: homopolymer
Location inside paper: abstract
Trivial name: glucan, β-1,3-glucan, curdlan, curdlan-type polysaccharide 13140, paramylon, curdlan, laminarin, β-glucan, curdlan, β-(1,3)-glucan, β-(1,3)-glucan, curdlan, curdlan, β-1,3-glucan, paramylon, reserve polysaccharide, b-glucan, β-1,3-D-glucan, laminaran, botryosphaeran, laminaran type β-D-glucan, latiglucan I, pachymaran, Curdlan, zymosan A, β-glucan, curdlan, laminarin, zymosan, zymosan, glucan particles, zymosan, β-(1-3)-glucan, β-(1,3)-glucan, β-(1,3)glucan, pachymaran, D-glucan (DPn)540, pachyman, laminaran, curdlan, zymosan, zymosan, β-(1,3)-glucan, zymosan A, zymosan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, pachyman, β-(1,3)-glucan, curdlan, callose, a water-insoluble β-(1→3)-glucan, fermentum β-polysaccharide, water-insoluble glucan, alkali-soluble β-glucan (PeA3), alkali-soluble polysaccharide (PCAP), callose, laminarin
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, lipophosphoglycan, glycoprotein, LPG, glucan, polysaccharide, glycoside, β-glucan, β3-glucan, cell wall glucan
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Synthetic data: enzymatic in vivo
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 5476,
746128,
4932,
5207Reference(s) to other database(s): GTC:G51056AN, GlycomeDB:
157, CCSD:
50049, CBank-STR:4225, CA-RN: 51052-65-4, GenDB:FJ3380871.1
Show glycosyltransferases
There is only one chemically distinct structure: