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Literature summary for 2.4.1.4 extracted from

  • Daude, D.; Champion, E.; Morel, S.; Guieysse, D.; Remaud-Simeon, M.; Andre, I.
    Probing substrate promiscuity of amylosucrase from Neisseria polysaccharea (2013), ChemCatChem, 5, 2288-2295.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Neisseria polysaccharea Q9ZEU2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of enzyme substrate specificity, from 11 potential donors harboring selective derivatizations that are experimentally evaluated, only 4-nitrophenyl-alpha-D-glucopyranoside is used by the wild-type enzyme, and this underlines the high specificity of the -1 subsite of enzyme NpAS for glucosyl donor substrates. Acceptor substrate promiscuity is explored by screening 20 hydroxylated molecules, including D- and L-monosaccharides as well as polyols. With the exception of one compound, all are successfully glucosylated, and showig the tremendous plasticity of the +1 subsite of NpAS, which is responsible for acceptor recognition. Acceptor substrates are arabinose, galactose, altrose, fucose, xylose, allose, mannose, D-sorbitol, Darabitol, D-mannitol, xylitol, myo-inositol, and maltitol. Analysis of product structures and enzyme enantiopreference by in silico docking analyses. The enzyme is able to discriminate very similar molecules such as enantiomers. Arabinose and altrose are more efficiently glucosylated by NpAS in their L forms, whereas xylose is better recognized in its D form. Glucosylation of mannose, xylose, and galactose are less discriminant, while the enzyme isstrictly enantiospecific toward D-fucose Neisseria polysaccharea ?
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Synonyms

Synonyms Comment Organism
NPAS
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Neisseria polysaccharea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Neisseria polysaccharea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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assay at Neisseria polysaccharea