1,3-Beta-glucan synthase

(Redirected from EC 2.4.1.34)

1,3-Beta-glucan synthase is a glucosyltransferase enzyme involved in the generation of beta-glucan in fungi. It serves as a pharmacological target for antifungal drugs such as caspofungin, anidulafungin, and micafungin, deemed 1,3-Beta-glucan synthase inhibitors. Under the CAZy classification system, fungi and plant members fall in the glycosyltransferase 48 family (GT48).[2] Some members of the glycosyltransferase 2 family (Pfam PF13632), such as the curdlan synthase CrdS (Q9X2V0), also has a similar activity.[3]

1,3-Beta-glucan synthase
Identifiers
EC no.2.4.1.34
CAS no.9037-30-3
Alt. namesGS-II,[1] paramylon synthetase,[1] callose synthase [1]
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Glycosyl transferase, family 48 (GT48)
Identifiers
SymbolGlucan_synthase
PfamPF02364
Pfam clanCL0111
InterProIPR003440
CAZyGT48
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The biosynthesis of disaccharides, oligosaccharides, and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

The family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2, and Gls3 from yeast. 1,3-Beta-glucan synthase (EC 2.4.1.34.) also known as callose synthase catalyses the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall.[4] The reaction catalysed is:

UDP-glucose + {(1,3)-beta-D-glucosyl}(N) = UDP + {(1,3)-beta-D-glucosyl}(N+1).

See also

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References

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  1. ^ a b c KFLGG, ENZYME: 2.4.1.34
  2. ^ Campbell JA, Davies GJ, Bulone V, Henrissat B (September 1997). "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities". Biochem. J. 326 (3): 929–39. doi:10.1042/bj3260929u. PMC 1218753. PMID 9334165.
  3. ^ Karnezis T, Epa VC, Stone BA, Stanisich VA (2003). "Topological characterization of an inner membrane (1→3)-beta-D-glucan (curdlan) synthase from Agrobacterium sp. strain ATCC31749". Glycobiology. 13 (10): 693–706. doi:10.1093/glycob/cwg093. PMID 12851288.
  4. ^ Mio T, Adachi-Shimizu M, Tachibana Y, Tabuchi H, Inoue SB, Yabe T, Yamada-Okabe T, Arisawa M, Watanabe T, Yamada-Okabe H (July 1997). "Cloning of the Candida albicans homolog of Saccharomyces cerevisiae GSC1/FKS1 and its involvement in beta-1,3-glucan synthesis". J. Bacteriol. 179 (13): 4096–105. doi:10.1128/jb.179.13.4096-4105.1997. PMC 179227. PMID 9209021.
This article incorporates text from the public domain Pfam and InterPro: IPR003440