The Enzyme Database

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EC 1.1.1.425     
Accepted name: levoglucosan dehydrogenase
Reaction: levoglucosan + NAD+ = 3-dehydrolevoglucosan + NADH + H+
Glossary: levoglucosan = 1,6-anhydro-β-D-glucopyranose
Other name(s): 1,6-anhydro-β-D-glucose dehydrogenase
Systematic name: 1,6-anhydro-β-D-glucopyranose:NAD+ 3-oxidoreductase
Comments: Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans. cf. EC 2.7.1.232, levoglucosan kinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nakahara, K., Kitamura, Y., Yamagishi, Y., Shoun, H. and Yasui, T. Levoglucosan dehydrogenase involved in the assimilation of levoglucosan in Arthrobacter sp. I-552. Biosci. Biotechnol. Biochem. 58 (1994) 2193–2196. [DOI] [PMID: 7765713]
2.  Sugiura, M., Nakahara, M., Yamada, C., Arakawa, T., Kitaoka, M. and Fushinobu, S. Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase. J. Biol. Chem. 293 (2018) 17375–17386. [DOI] [PMID: 30224354]
[EC 1.1.1.425 created 2021]
 
 
EC 2.7.1.232     
Accepted name: levoglucosan kinase
Reaction: ATP + levoglucosan + H2O = ADP + D-glucose 6-phosphate
Glossary: levoglucosan = 1,6-anhydro-β-D-glucopyranose
Systematic name: ATP:1,6-anhydro-β-D-glucopyranose 6-phosphotransferase (hydrolyzing)
Comments: Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. The enzyme, found in yeast and fungi, requires a magnesium ion. cf. EC 1.1.1.425, levoglucosan dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhuang, X. and Zhang, H. Identification, characterization of levoglucosan kinase, and cloning and expression of levoglucosan kinase cDNA from Aspergillus niger CBX-209 in Escherichia coli. Protein Expr. Purif. 26 (2002) 71–81. [PMID: 12356473]
2.  Dai, J., Yu, Z., He, Y., Zhang, L., Bai, Z., Dong, Z., Du, Y. and Zhang, H. Cloning of a novel levoglucosan kinase gene from Lipomyces starkeyi and its expression in Escherichia coli. World J. Microbiol. Biotechnol. 25 (2009) 1589–1595. [DOI]
3.  Layton, D.S., Ajjarapu, A., Choi, D.W. and Jarboe, L.R. Engineering ethanologenic Escherichia coli for levoglucosan utilization. Bioresour. Technol. 102 (2011) 8318–8322. [DOI] [PMID: 21719279]
4.  Islam, Z.U., Zhisheng, Y., Hassan el, B., Dongdong, C. and Hongxun, Z. Microbial conversion of pyrolytic products to biofuels: a novel and sustainable approach toward second-generation biofuels. J. Ind. Microbiol. Biotechnol. 42 (2015) 1557–1579. [DOI] [PMID: 26433384]
5.  Bacik, J.P., Klesmith, J.R., Whitehead, T.A., Jarboe, L.R., Unkefer, C.J., Mark, B.L. and Michalczyk, R. Producing glucose 6-phosphate from cellulosic biomass: structural insights into levoglucosan bioconversion. J. Biol. Chem. 290 (2015) 26638–26648. [DOI] [PMID: 26354439]
[EC 2.7.1.232 created 2021]
 
 


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