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Results 1 - 10 of 12 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.162-deoxy-2-fluoro-alpha-maltosyl fluoride + maltotetraose - Streptomyces coelicolor ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n - Mycolicibacterium smegmatis phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n - Streptomyces coelicolor phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose Mycolicibacterium smegmatis phosphate + [(1->4)-alpha-D-glucosyl]n+2 - r
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n acceptor and secondary binding sites are identified. The sugar residues in the acceptor subsites +1 to +5 are oriented such that they disfavor the binding of malto-oligosaccharides that bear branches at their 6-positions, consistent with the known acceptor chain specificity of GlgE. A secondary binding site remote from the catalytic center is identified. This site is capable of binding a branched alpha-glucan and is most likely involved in guiding acceptors toward the donor site because its disruption kinetically compromises the ability of GlgE to extend polymeric substrates Streptomyces coelicolor phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n - Mycolicibacterium smegmatis ATCC 14468 phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose Mycolicibacterium smegmatis ATCC 14468 phosphate + [(1->4)-alpha-D-glucosyl]n+2 - r
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n - Streptomyces coelicolor ATCC BAA-471 phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n acceptor and secondary binding sites are identified. The sugar residues in the acceptor subsites +1 to +5 are oriented such that they disfavor the binding of malto-oligosaccharides that bear branches at their 6-positions, consistent with the known acceptor chain specificity of GlgE. A secondary binding site remote from the catalytic center is identified. This site is capable of binding a branched alpha-glucan and is most likely involved in guiding acceptors toward the donor site because its disruption kinetically compromises the ability of GlgE to extend polymeric substrates Streptomyces coelicolor ATCC BAA-471 phosphate + [(1->4)-alpha-D-glucosyl]n+2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.16more GMPMT requires a high-molecular weight alpha-1,4-glucan as the acceptor. The enzyme can also transfer maltosyl units to maltosaccharides, e.g. maltotetraose to maltohexaose, overview Mycolicibacterium smegmatis ? - ?
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