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ENZYME entry: EC 3.2.1.6

Accepted Name
Endo-1,3(4)-beta-glucanase.
Alternative Name(s)
Endo-1,3-beta-glucanase.
Endo-1,4-beta-glucanase.
Laminarinase.
Reaction catalysed
Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3
Comment(s)
  • Substrates include laminarin, lichenin and cereal D-glucans.
  • Different from EC 3.2.1.39 and EC 3.2.1.52.
Cross-references
PROSITEPDOC00794
BRENDA3.2.1.6
EC2PDB3.2.1.6
ExplorEnz3.2.1.6
PRIAM enzyme-specific profiles3.2.1.6
KEGG Ligand Database for Enzyme Nomenclature3.2.1.6
IUBMB Enzyme Nomenclature3.2.1.6
IntEnz3.2.1.6
MEDLINEFind literature relating to 3.2.1.6
MetaCyc3.2.1.6
UniProtKB/Swiss-Prot
D4AJR9, EGLX_ARTBC;  A1C7B5, EGLX_ASPCL;  B0XTU6, EGLX_ASPFC;  
B8N7S7, EGLX_ASPFN;  Q4X084, EGLX_ASPFU;  A2QBQ3, EGLX_ASPNC;  
Q2UIE6, EGLX_ASPOR;  Q5BAP5, EGLX_EMENI;  A1DHY9, EGLX_NEOFI;  
D4AZ24, ENG1_ARTBC;  Q5AIR7, ENG1_CANAL;  Q9UT45, ENG1_SCHPO;  
P53753, ENG1_YEAST;  Q09850, ENG2_SCHPO;  Q12168, ENG2_YEAST;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-