Lichenase

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Licheninase
Licheninase
Identifiers
EC no.	3.2.1.73
CAS no.	37288-51-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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NCBI	proteins

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).

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]

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

^ Barras DR, Moore AE, Stone BA (1969). "Enzyme-Substrate Relationships Among β-Glucan Hydrolases". Cellulases and Their Applications. Advances in Chemistry. Vol. 95. pp. 105–138. doi:10.1021/ba-1969-0095.ch008. ISBN 0-8412-0095-5.
^ "Lichenase endo-1-3-1-4-beta-D-Glucanase Bacillus subtilis". megazyme.com. Retrieved 2019-06-25.
^ 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. Bibcode:1991JSFA...55..303M. doi:10.1002/jsfa.2740550215. ISSN 0022-5142.
^ 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.
^ 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.
^ 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
^ McCleary, Barry V. (1988-01-01). "Lichenase from Bacillus subtilis". Biomass Part A: Cellulose and Hemicellulose. Methods in Enzymology. Vol. 160. Academic Press. pp. 572–575. doi:10.1016/0076-6879(88)60170-4. ISBN 9780121820619.
^ 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.
^ 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. Bibcode:1995FEBSL.374..221H. doi:10.1016/0014-5793(95)01111-Q. PMID 7589539.
^ 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-β-D-glucanase from Fibrobacter succinogenes". Journal of Molecular Biology. 330 (3): 607–620. doi:10.1016/S0022-2836(03)00630-2. PMID 12842475.
^ ^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

Licheninase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Barras DR, Moore AE, Stone BA (1969). "Enzyme-Substrate Relationships Among β-Glucan Hydrolases". Cellulases and Their Applications. Advances in Chemistry. Vol. 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. Bibcode:1991JSFA...55..303M. 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. Vol. 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. Bibcode:1995FEBSL.374..221H. 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-β-D-glucanase from Fibrobacter succinogenes". Journal of Molecular Biology. 330 (3): 607–620. doi:10.1016/S0022-2836(03)00630-2. PMID 12842475.

[:0-11] 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.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)