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Literature summary extracted from

  • Roujeinikova, A.; Raasch, C.; Burke, J.; Baker, P.; Liebl, W.; Rice, D.
    The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity (2001), J. Mol. Biol., 312, 119-131 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.99.16 crystal structures of the enzyme and its complex with maltose are determined at 2.4 A and 2.1 A resolution. Crystals belong to space group P4(1)22 with unit-cell dimensions a = b = 148.7 A, c = 106.7 A Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.16 Thermotoga maritima O33838
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.16 additional information 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 Thermotoga maritima ?
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Subunits

EC Number Subunits Comment Organism
2.4.99.16 homodimer each subunit consists of four domains Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
2.4.99.16 maltosyltransferase
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 Thermotoga maritima