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| 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 | ||||||||
| |||||||||
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).
This enzyme catalyses hydrolysis of β-(1,4)-D-glucosidic linkages in mixed-linkage glucans containing both (1,3)- and (1,4)-bonds
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]
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]
- ^ 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.
- Licheninase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This article needs additional or more specific
categories. (April 2024) |
(Redirected from
Licheninase)
| This article has multiple issues. Please help
improve it or discuss these issues on the
talk page. (
Learn how and when to remove these template messages)
|
| 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 | ||||||||
| |||||||||
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).
This enzyme catalyses hydrolysis of β-(1,4)-D-glucosidic linkages in mixed-linkage glucans containing both (1,3)- and (1,4)-bonds
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]
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]
- ^ 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.
- Licheninase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| This article needs additional or more specific
categories. (April 2024) |