2.4.99.16: starch synthase (maltosyl-transferring)
This is an abbreviated version!
For detailed information about starch synthase (maltosyl-transferring), go to the full flat file.
Word Map on EC 2.4.99.16
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2.4.99.16
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tuberculosis
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glycogen
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coelicolor
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trehalose
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cyclodextrins
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maltooligosaccharides
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antituberculosis
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venezuelae
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actinomycetes
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disaccharide
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glycogen-like
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capsular
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smegmatis
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drug development
- 2.4.99.16
- tuberculosis
- glycogen
- coelicolor
- trehalose
- cyclodextrins
- maltooligosaccharides
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antituberculosis
- venezuelae
- actinomycetes
- disaccharide
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glycogen-like
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capsular
- smegmatis
- drug development
Reaction
Synonyms
alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase, alpha1,4-glucan:maltose-1-P maltosyltransferase, GlgE, GlgE isoform I, GMPMT, maltosyl transferase, maltosyltransferase, maltosyltransferase GlgE
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Substrates Products
Substrates Products on EC 2.4.99.16 - starch synthase (maltosyl-transferring)
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REACTION DIAGRAM
2-deoxy-2-fluoro-alpha-maltosyl fluoride + maltotetraose
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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r
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides or glucose. Analysis of maltose binding in the active site reveals that the transfer of dextrinyl residues longer than a maltosyl unit is prevented by termination of the active-site cleft after the -2 subsite by the side-chain of Lys151 and the stretch of residues 314-317, providing an explanation for the strict transfer specificity of MTase
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