ExplorEnz: EC 1.1.2.11

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1.1.2.11

Accepted name:

glucoside 3-dehydrogenase (cytochrome c)

Reaction:

a D-glucoside + a ferric c-type cytochrome = a 3-dehydro-D-glucoside + a ferrous c-type cytochrome

Other name(s):

D-glucoside 3-dehydrogenase (ambiguous); D-aldohexopyranoside dehydrogenase (ambiguous); D-aldohexoside:cytochrome c oxidoreductase; hexopyranoside-cytochrome c oxidoreductase

Systematic name:

a D-glucoside:ferric c-type cytochrome 3-oxidoreductase

Comments:

This bacterial enzyme acts on D-glucose, D-galactose, D-glucosides and D-galactosides, but the best substrates are disaccharides with a glucose moiety at the non-reducing end. It consists of two subunits, a catalytic subunit that contains an FAD cofactor and an iron-sulfur cluster, and a "hitch-hiker" subunit containing a signal peptide for translocation into the periplasm. A dedicated c-type cytochrome protein serves as an electron acceptor, transferring the electrons from the catalytic subunit to the cell's electron transfer chain. cf. EC 1.1.99.13, glucoside 3-dehydrogenase (acceptor).

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc

References:

1.	Hayano, K. and Fukui, S. Purification and properties of 3-ketosucrose-forming enzyme from the cells of Agrobacterium tumefaciens. J. Biol. Chem. 242 (1967) 3665–3672. [PMID: 6038493]
2.	Nakamura, L.K. and Tyler, D.D. Induction of D-aldohexoside:cytochrome c oxidoreductase in Agrobacterium tumefaciens. J. Bacteriol. 129 (1977) 830–835. [DOI] [PMID: 838689]
3.	Takeuchi, M., Ninomiya, K., Kawabata, K., Asano, N., Kameda, Y. and Matsui, K. Purification and properties of glucoside 3-dehydrogenase from Flavobacterium saccharophilum. J. Biochem. 100 (1986) 1049–1055. [DOI] [PMID: 3818559]
4.	Takeuchi, M., Asano, N., Kameda, Y. and Matsui, K. Physiological role of glucoside 3-dehydrogenase and cytochrome c₅₅₁ in the sugar oxidizing system of Flavobacterium saccharophilum. J. Biochem. 103 (1988) 938–943. [DOI] [PMID: 2844746]
5.	Tsugawa, W., Horiuchi, S., Tanaka, M., Wake, H. and Sode, K. Purification of a marine bacterial glucose dehydrogenase from Cytophaga marinoflava and its application for measurement of 1,5-anhydro-D-glucitol. Appl. Biochem. Biotechnol. 56 (1996) 301–310. [DOI] [PMID: 8984902]
6.	Kojima, K., Tsugawa, W. and Sode, K. Cloning and expression of glucose 3-dehydrogenase from Halomonas sp. α-15 in Escherichia coli. Biochem. Biophys. Res. Commun. 282 (2001) 21–27. [DOI] [PMID: 11263965]
7.	Zhang, J.F., Zheng, Y.G., Xue, Y.P. and Shen, Y.C. Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024. Appl. Microbiol. Biotechnol. 71 (2006) 638–645. [DOI] [PMID: 16292530]
8.	Zhang, J.F., Chen, W.Q. and Chen, H. Gene cloning and expression of a glucoside 3-dehydrogenase from Sphingobacterium faecium ZJF-D6, and used it to produce N-p-nitrophenyl-3-ketovalidamine. World J. Microbiol. Biotechnol. 33:21 (2017). [DOI] [PMID: 28044272]
9.	Miyazaki, R., Yamazaki, T., Yoshimatsu, K., Kojima, K., Asano, R., Sode, K. and Tsugawa, W. Elucidation of the intra- and inter-molecular electron transfer pathways of glucoside 3-dehydrogenase. Bioelectrochemistry 122 (2018) 115–122. [DOI] [PMID: 29625423]

[EC 1.1.2.11 created 2022]