The Enzyme Database

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EC 3.2.1.6     
Accepted name: endo-1,3(4)-β-glucanase
Reaction: Endohydrolysis of (1→3)- or (1→4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3
Other name(s): endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3(4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1→3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3;1,4)-β-D-glucan 3(4)-glucanohydrolase
Systematic name: 3(or 4)-β-D-glucan 3(4)-glucanohydrolase
Comments: Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 β-N-acetylhexosaminidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-14-3
References:
1.  Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases. Biochim. Biophys. Acta 191 (1969) 329–341. [PMID: 5354264]
2.  Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase. Biochim. Biophys. Acta 191 (1969) 342–353. [PMID: 5354265]
3.  Cunningham, L.W. and Manners, D.J. Enzymic degradation of lichenin. Biochem. J. 80 (1961) 42.
4.  Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895]
5.  Sova, V.V., Elyakova, L.A. and Vaskovsky, V.E. Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis. Biochim. Biophys. Acta 212 (1970) 111–115. [PMID: 5500926]
[EC 3.2.1.6 created 1961, modified 1976]
 
 


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