| 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, PDB, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 5500926] |
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| [EC 3.2.1.6 created 1961, modified 1976] |
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