(1-4)-a-D-glucan 1-a-D-glucosylmutase

(1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase (EC 5.4.99.15, malto-oligosyltrehalose synthase, maltodextrin alpha-D-glucosyltransferase) is an enzyme with systematic name (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose

\rightleftharpoons

1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside

The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units.

References

↑ Maruta, K., Nakada, T., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. (1995). "Formation of trehalose from maltooligosaccharides by a novel enzymatic system". Biosci. Biotechnol. Biochem. 59: 1829–1834. doi:10.1271/bbb.59.1829. PMID 8534970.
↑ Nakada, T., Maruta, K., Tsusaki, K., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. (1995). "Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36". Biosci. Biotechnol. Biochem. 59: 2210–2214. doi:10.1271/bbb.59.2210. PMID 8611744.
↑ Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. (1996). "Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius". Biosci. Biotechnol. Biochem. 60: 263–266. doi:10.1271/bbb.60.263. PMID 9063973.

External links

[//www.nlm.nih.gov/cgi/mesh/2011/MB_cgi?mode=&term=(1->4)-alpha-D-glucan+1-alpha-D-glucosylmutase (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase] at the US National Library of Medicine Medical Subject Headings (MeSH)

Isomerase: mutases (EC 5.4)

5.4.1 Acyl Groups	Lysolecithin acylmutase Precorrin-8X methylmutase

5.4.2 Phosphomutases	Phosphoglycerate mutase Bisphosphoglycerate mutase Phosphoglucomutase Phosphomannomutase PMM1 PMM2

5.4.99 Other groups	Methylmalonyl-CoA mutase Lanosterol synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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