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Lichenase
Type of enzyme From Wikipedia, the free encyclopedia
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Lichenase (EC 3.2.1.73, licheninase, β-(1→4)-D-glucan 4-glucanohydrolase, 1,3, 1,4-β-glucan endohydrolase, 1,3, 1,4-β-glucan 4-glucanohydrolase, 1,3-1,4-β-D-glucan 4-glucanohydrolase) is an enzyme with systematic name (1→3)-(1→4)-β-D-glucan 4-glucanohydrolase.[1][2] It was named after its activity in on lichenin (a form of mixed-linkage glucan).
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Activity
This enzyme catalyses hydrolysis of β-(1,4)-D-glucosidic linkages in mixed-linkage glucans containing both (1,3)- and (1,4)-bonds
Specificity
The best-characterised variant of this of enzyme is Bacillus subtilis lichenase, which is used as a molecular biology tool in determining the structure of mixed-linkage glucans.[3][4][5][6] This variant cleaves (1,4) bonds that immediately follow a (1,3) bond.[7]
Other lichenases have different specificities, for example Aspergillus japonicus lichenase cleaves (1,4) bonds that immediately precede a (1,3) bond.[8]
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Structure
Lichenases are from glycoside hydrolase family 16, and share a jellyroll structure.[9][10][11] A deep surface cleft acts as the substrate binding site.[11]
References
External links
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