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Literature summary extracted from

  • Syson, K.; Stevenson, C.E.; Miah, F.; Barclay, J.E.; Tang, M.; Gorelik, A.; Rashid, A.M.; Lawson, D.M.; Bornemann, S.
    Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE (2016), J. Biol. Chem., 291, 21531-21540 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n Streptomyces coelicolor
-
 phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n Streptomyces coelicolor ATCC BAA-471
-
 phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.16 Streptomyces coelicolor Q9L1K2
-
-
2.4.99.16 Streptomyces coelicolor ATCC BAA-471 Q9L1K2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
-
 Streptomyces coelicolor phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?
2.4.99.16 alpha-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
-
 ?
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
-
 Streptomyces coelicolor ATCC BAA-471 phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?
2.4.99.16 alpha-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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.99.16 alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase
-
 Streptomyces coelicolor
2.4.99.16 maltosyltransferase GlgE
-
 Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
2.4.99.16 drug target the enzyme has been genetically validated as a target for tuberculosis therapies Streptomyces coelicolor
2.4.99.16 metabolism the enzyme is involved inx02alpha-glucan biosynthesis in bacteria Streptomyces coelicolor