Lichenase

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{{Infobox enzyme

| Name = Licheninase

| EC_number = 3.2.1.73

| CAS_number = 37288-51-0

| GO_code =

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Lichenase ({{EnzExplorer|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.{{cite book | title = Cellulases and Their Applications| vauthors = Barras DR, Moore AE, Stone BA |year = 1969 |volume = 95 |pages = 105–138 | doi = 10.1021/ba-1969-0095.ch008 | chapter = Enzyme-Substrate Relationships Among β-Glucan Hydrolases | series = Advances in Chemistry | isbn = 0-8412-0095-5 }}{{Cite web|url=https://secure.megazyme.com/Lichenase-endo-1-3-4-Beta-D-Glucanase-Bacillus-sp|title=Lichenase endo-1-3-1-4-beta-D-Glucanase Bacillus subtilis|website=megazyme.com|access-date=2019-06-25}} 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.{{Cite journal|last1=McCleary|first1=Barry V|last2=Codd|first2=Rachel|date=1991|title=Measurement of (1 → 3),(1 → 4)-β-D-glucan in barley and oats: A streamlined enzymic procedure|journal=Journal of the Science of Food and Agriculture|volume=55|issue=2|pages=303–312|doi=10.1002/jsfa.2740550215|bibcode=1991JSFA...55..303M |issn=0022-5142}}{{Cite journal|last1=Mangan|first1=D.|last2=Liadova|first2=A.|last3=Ivory|first3=R.|last4=McCleary|first4=B. V.|date=2016-11-29|title=Novel approaches to the automated assay of β-glucanase and lichenase activity|journal=Carbohydrate Research|volume=435|pages=162–172|doi=10.1016/j.carres.2016.10.006|pmid=27810709|issn=0008-6215}}{{Cite journal|last1=Yoo|first1=Dong-Hyung|last2=Lee|first2=Byung-Hoo|last3=Chang|first3=Pahn-Shick|last4=Lee|first4=Hyeon Gyu|last5=Yoo|first5=Sang-Ho|date=2007-03-01|title=Improved Quantitative Analysis of Oligosaccharides from Lichenase-Hydrolyzed Water-Soluble Barley β-Glucans by High-Performance Anion-Exchange Chromatography|journal=Journal of Agricultural and Food Chemistry|volume=55|issue=5|pages=1656–1662|doi=10.1021/jf062603l|pmid=17284049|bibcode=2007JAFC...55.1656Y |issn=0021-8561}}{{Citation|last1=Hrmova|first1=Maria|title=Chapter 3.1 - Plant and Microbial Enzymes Involved in the Depolymerization of (1,3)-β-D-Glucans and Related Polysaccharides|date=2009-01-01|doi=10.1016/B978-0-12-373971-1.00004-2|work=Chemistry, Biochemistry, and Biology of 1-3 Beta Glucans and Related Polysaccharides|pages=119–170|editor-last=Bacic|editor-first=Antony|publisher=Academic Press|isbn=9780123739711|last2=Fincher|first2=Geoffrey B.|editor2-last=Fincher|editor2-first=Geoffrey B.|editor3-last=Stone|editor3-first=Bruce A.}} This variant cleaves (1,4) bonds that immediately follow a (1,3) bond.{{cite book |last=McCleary|first=Barry V. |date=1988-01-01 |volume=160|pages=572–575 |publisher=Academic Press|doi=10.1016/0076-6879(88)60170-4 |isbn=9780121820619|chapter=Lichenase from Bacillus subtilis |title=Biomass Part A: Cellulose and Hemicellulose |series=Methods in Enzymology }}

Other lichenases have different specificities, for example Aspergillus japonicus lichenase cleaves (1,4) bonds that immediately precede a (1,3) bond.{{Cite journal|last1=Grishutin|first1=Sergei G.|last2=Gusakov|first2=Alexander V.|last3=Dzedzyulya|first3=Ekaterina I.|last4=Sinitsyn|first4=Arkady P.|date=2006|title=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|journal=Carbohydrate Research|language=en|volume=341|issue=2|pages=218–229|doi=10.1016/j.carres.2005.11.011|pmid=16343463}}

Structure

Lichenases are from glycoside hydrolase family 16, and share a jellyroll structure.{{Cite journal|last1=Hahn|first1=Michael|last2=Pons|first2=Jaume|last3=Planas|first3=Antoni|last4=Querol|first4=Enrique|last5=Heinemann|first5=Udo|date=1995-10-30|title=Crystal structure of Bacillus licheniformis 1,3-1,4-β- d -glucan 4-glucanohydrolase at 1.8 Å resolution|journal=FEBS Letters|language=en|volume=374|issue=2|pages=221–224|doi=10.1016/0014-5793(95)01111-Q|pmid=7589539|doi-access=free|bibcode=1995FEBSL.374..221H }}{{Cite journal|journal=Journal of Molecular Biology| title=Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-β-D-glucanase from Fibrobacter succinogenes|last1=Tsai|first1=L.-C.|last2=Shyur|first2=L.-F.|date=2003-07-15|last3=Lee|first3=S.-H.|last4=Lin|first4=S.-S.|last5=Yuan|first5=H.S.| volume=330| issue=3| pages=607–620|doi = 10.1016/S0022-2836(03)00630-2| pmid=12842475}}{{Cite journal|last1=Furtado|first1=Gilvan Pessoa|last2=Ribeiro|first2=Lucas Ferreira|last3=Santos|first3=Camila Ramos|last4=Tonoli|first4=Celisa Caldana|last5=de Souza|first5=Angelica Rodrigues|last6=Oliveira|first6=Renata Rocha|last7=Murakami|first7=Mario Tyago|last8=Ward|first8=Richard John|date=2011-05-01|title=Biochemical and structural characterization of a β-1,3–1,4-glucanase from Bacillus subtilis 168|journal=Process Biochemistry|volume=46|issue=5|pages=1202–1206|doi=10.1016/j.procbio.2011.01.037|issn=1359-5113|doi-access=free}} A deep surface cleft acts as the substrate binding site.

References

External links

{{MeshName|Licheninase}}

Category:EC 3.2.1