(1-3)-(1-4)-beta-D-glucan 4-glucanohydrolase

Licheninase
Identifiers
EC number3.2.1.73
CAS number37288-51-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Lichenase (EC 3.2.1.73, licheninase, beta-(1->4)-D-glucan 4-glucanohydrolase, 1,3, 1,4-beta-glucan endohydrolase, 1,3, 1,4-beta-glucan 4-glucanohydrolase, 1,3-1,4-beta-D-glucan 4-glucanohydrolase) is an enzyme with systematic name (1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase.[1][2] It was named after its activity in on lichenin (a form of mixed-linkage glucan).

Activity[]

This enzyme catalyses the following chemical reaction

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]

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[]

  1. ^ Barras DR, Moore AE, Stone BA (1969). "Enzyme-Substrate Relationships Among β-Glucan Hydrolases". Cellulases and Their Applications. Advances in Chemistry. 95. pp. 105–138. doi:10.1021/ba-1969-0095.ch008. ISBN 0-8412-0095-5.
  2. ^ "Lichenase endo-1-3-1-4-beta-D-Glucanase Bacillus subtilis". megazyme.com. Retrieved 2019-06-25.
  3. ^ McCleary, Barry V; Codd, Rachel (1991). "Measurement of (1 → 3),(1 → 4)-β-D-glucan in barley and oats: A streamlined enzymic procedure". Journal of the Science of Food and Agriculture. 55 (2): 303–312. doi:10.1002/jsfa.2740550215. ISSN 0022-5142.
  4. ^ Mangan, D.; Liadova, A.; Ivory, R.; McCleary, B. V. (2016-11-29). "Novel approaches to the automated assay of β-glucanase and lichenase activity". Carbohydrate Research. 435: 162–172. doi:10.1016/j.carres.2016.10.006. ISSN 0008-6215. PMID 27810709.
  5. ^ Yoo, Dong-Hyung; Lee, Byung-Hoo; Chang, Pahn-Shick; Lee, Hyeon Gyu; Yoo, Sang-Ho (2007-03-01). "Improved Quantitative Analysis of Oligosaccharides from Lichenase-Hydrolyzed Water-Soluble Barley β-Glucans by High-Performance Anion-Exchange Chromatography". Journal of Agricultural and Food Chemistry. 55 (5): 1656–1662. doi:10.1021/jf062603l. ISSN 0021-8561. PMID 17284049.
  6. ^ Hrmova, Maria; Fincher, Geoffrey B. (2009-01-01), Bacic, Antony; Fincher, Geoffrey B.; Stone, Bruce A. (eds.), "Chapter 3.1 - Plant and Microbial Enzymes Involved in the Depolymerization of (1,3)-β-d-Glucans and Related Polysaccharides", Chemistry, Biochemistry, and Biology of 1-3 Beta Glucans and Related Polysaccharides, Academic Press, pp. 119–170, doi:10.1016/B978-0-12-373971-1.00004-2, ISBN 9780123739711
  7. ^ McCleary, Barry V. (1988-01-01). "Lichenase from Bacillus subtilis". Biomass Part A: Cellulose and Hemicellulose. Methods in Enzymology. 160. Academic Press. pp. 572–575. doi:10.1016/0076-6879(88)60170-4. ISBN 9780121820619.
  8. ^ Grishutin, Sergei G.; Gusakov, Alexander V.; Dzedzyulya, Ekaterina I.; Sinitsyn, Arkady P. (2006). "A lichenase-like family 12 endo-(1→4)-β-glucanase from Aspergillus japonicus: study of the substrate specificity and mode of action on β-glucans in comparison with other glycoside hydrolases". Carbohydrate Research. 341 (2): 218–229. doi:10.1016/j.carres.2005.11.011. PMID 16343463.
  9. ^ Hahn, Michael; Pons, Jaume; Planas, Antoni; Querol, Enrique; Heinemann, Udo (1995-10-30). "Crystal structure of Bacillus licheniformis 1,3-1,4-β- d -glucan 4-glucanohydrolase at 1.8 Å resolution". FEBS Letters. 374 (2): 221–224. doi:10.1016/0014-5793(95)01111-Q. PMID 7589539.
  10. ^ Tsai, L.-C.; Shyur, L.-F.; Lee, S.-H.; Lin, S.-S.; Yuan, H.S. (2003-07-15). "Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes". doi:10.2210/pdb1mve/pdb. Cite journal requires |journal= (help)
  11. ^ a b Furtado, Gilvan Pessoa; Ribeiro, Lucas Ferreira; Santos, Camila Ramos; Tonoli, Celisa Caldana; de Souza, Angelica Rodrigues; Oliveira, Renata Rocha; Murakami, Mario Tyago; Ward, Richard John (2011-05-01). "Biochemical and structural characterization of a β-1,3–1,4-glucanase from Bacillus subtilis 168". Process Biochemistry. 46 (5): 1202–1206. doi:10.1016/j.procbio.2011.01.037. ISSN 1359-5113.

External links[]