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MalQ N-terminal beta sandwich domain
Amylomaltase MalQ is essential for the metabolism of maltose and maltodextrins in Escherichia coli. It catalyzes transglycosylation/disproportionation reactions in which glycosyl or dextrinyl units are transferred among linear maltodextrins of various lengths [2]. This domain called N2 resembles a beta-sandwich consisting of a five-stranded mixed beta-sheet and a short two-stranded antiparallel beta-sheet. The N2 structure is reminiscent of carbohydrate-binding modules (CBMs) [2]. However, a comparison with structurally known CBMs did not reveal significant similarities. Paper describing PDB structure 3faw. [1]. 19329633. Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development. Gourlay LJ, Santi I, Pezzicoli A, Grandi G, Soriani M, Bolognesi M;. J Bacteriol. 2009;191:3544-3552. Paper describing PDB structure 4s3p. [2]. 26139606. Structural Basis for the Interconversion of Maltodextrins by MalQ, the Amylomaltase of Escherichia coli. Weiss SC, Skerra A, Schiefner A;. J Biol Chem. 2015;290:21352-21364. Paper describing PDB structure 5b68. [3]. 27366969. Crystal Structure of Amylomaltase from Corynebacterium glutamicum. Joo S, Kim S, Seo H, Kim KJ;. J Agric Food Chem. 2016;64:5662-5670. (from Pfam)
4-alpha-glucanotransferase
These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan [1]. [1]. 7678257. Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. Takaha T, Yanase M, Okada S, Smith SM;. J Biol Chem 1993;268:1391-1396. (from Pfam)
4-alpha-glucanotransferase transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
Amylomaltase; acts to release glucose from maltodextrins
This enzyme is known as amylomaltase and disproportionating enzyme.
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