Biology:(1-4)-a-D-glucan 1-a-D-glucosylmutase
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Short description: Class of enzymes
(1→4)-α-D-Glucan 1-α-D-glucosylmutase | |||||||||
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Identifiers | |||||||||
EC number | 5.4.99.15 | ||||||||
CAS number | 170780-49-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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(1→4)-α-D-Glucan 1-α-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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Formation of trehalose from maltooligosaccharides by a novel enzymatic system". Bioscience, Biotechnology, and Biochemistry 59 (10): 1829–34. October 1995. doi:10.1271/bbb.59.1829. PMID 8534970.
- ↑ "Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36". Bioscience, Biotechnology, and Biochemistry 59 (12): 2210–4. December 1995. doi:10.1271/bbb.59.2210. PMID 8611744.
- ↑ "Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius". Bioscience, Biotechnology, and Biochemistry 60 (2): 263–6. February 1996. doi:10.1271/bbb.60.263. PMID 9063973.
External links
- >4)-alpha-D-glucan%201-alpha-D-glucosylmutase (1->4)-alpha-D-glucan+1-alpha-D-glucosylmutase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/(1-4)-a-D-glucan 1-a-D-glucosylmutase.
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