MetaCyc EC 3.2.1.218 -- α-3′-ketoglucosidase

Parent Class: EC-Numbers3 -- Hydrolases3.2 -- Glycosylases3.2.1 -- Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds

Synonyms: 3'-keto-α-D-gluco-disaccharide hydrolase, α-3-ketoglucosidase (incorrect), 3-keto-glucoside hydrolase

Systematic Name: 3′-dehydrosucrose 3′-dehydroglucohydrolase

Unification Links: BRENDA:3.2.1.218, ENZYME:3.2.1.218, IUBMB-ExplorEnz:3.2.1.218

Reaction:
3'-dehydrosucrose + H2O → 3-dehydro-D-glucopyranose + D-fructofuranose

Unofficial Reactions:
3'-dehydro-α,α-trehalose + H2O → 3-dehydro-D-glucopyranose + D-glucopyranose,
3'-dehydromaltose + H2O → 3-dehydro-D-glucopyranose + D-glucopyranose

Enzymes and Genes:
α-3'-ketoglucosidase ( Agrobacterium tumefaciens )

Summary:
The enzyme, originally characterized from the bacterium Agrobacterium tumefaciens, is specific for 3'-dehydro-disaccharides that contain a 3-dehydro-α-D-glucose at the non-reducing end such as 3'-dehydrosucrose and 3'-dehydro-α,α-trehalose. It has no activity with disaccharides in which the glucose is in β conformation, and greatly reduced activity with disaccharides with an unmodified 3' position.

Citations: [Hayano70, Liu21a]


References

Hayano70: Hayano K, Fukui S (1970). "Alpha-3-ketoglucosidase of Agrobacterium tumefaciens." J Bacteriol 101(3);692-7. PMID: 5438043

Liu21a: Liu H, Shiver AL, Price MN, Carlson HK, Trotter VV, Chen Y, Escalante V, Ray J, Hern KE, Petzold CJ, Turnbaugh PJ, Huang KC, Arkin AP, Deutschbauer AM (2021). "Functional genetics of human gut commensal Bacteroides thetaiotaomicron reveals metabolic requirements for growth across environments." Cell Rep 34(9);108789. PMID: 33657378


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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