Levansucrase
Levansucrase (EC 2.4.1.10) is an enzyme that catalyzes the chemical reaction
- sucrose + (2,6-beta-D-fructosyl)n glucose + (2,6-beta-D-fructosyl)n+1
levansucrase | |||||||||
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Levansucrase monomer, Bacillus subtilis | |||||||||
Identifiers | |||||||||
EC number | 2.4.1.10 | ||||||||
CAS number | 9030-17-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Thus, the two substrates of this enzyme are sucrose and (2,6-beta-D-fructosyl)n, whereas its two products are glucose and (2,6-beta-D-fructosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:2,6-beta-D-fructan 6-beta-D-fructosyltransferase. Other names in common use include sucrose 6-fructosyltransferase, beta-2,6-fructosyltransferase, and beta-2,6-fructan:D-glucose 1-fructosyltransferase. This enzyme participates in starch and sucrose metabolism and two-component system - general.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1OYG, 1PT2, and 1W18.
References
- Hehre EJ (1951). "Enzymic synthesis of polysaccharides: a biological type of polymerization". Adv. Enzymol. Relat. Subj. Biochem. Advances in Enzymology - and Related Areas of Molecular Biology. 11: 297–337. doi:10.1002/9780470122563.ch6. ISBN 978-0-470-12256-3.
- AVIGAD G, FEINGOLD DS, HESTRIN S (1956). "The mechanism of polysaccharide production from sucrose. 3 Donor-acceptor specificity of levansucrase from Aerobacter levanicum". Biochem. J. 64 (2): 340–51. PMC 1199737. PMID 13363847.
- Reese ET, Avigad G (1966). "Purification of levansucrase by precipitation with levan". Biochim. Biophys. Acta. 113 (1): 79–83. doi:10.1016/s0926-6593(66)80123-6. PMID 5940635.