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Literature summary for 3.2.1.18 extracted from

  • Cheng, L.L.; Shidmoossavee, F.S.; Bennet, A.J.
    Neuraminidase substrate promiscuity permits a mutant Micromonospora viridifaciens enzyme to synthesize artificial carbohydrates (2014), Biochemistry, 53, 3982-3989.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y370G the mutation produces an efficient catalyst for the transfer of N-acetylneuraminic acid from an artificial substrate (i.e., phenyl N-acetyl-beta-D-neuraminide) to a sugar acceptor (e.g., D-lactose, D-glucose, D-mannose, D-raffinose, D-allose, or D-fructose) to give N-acetyl-alpha-neuraminide coupled carbohydrate products. In addition, this mutant enzyme catalyzes the transfer of a sugar residue from the artificial substrate 2-fluorophenyl N-acetyl-beta-D-neuraminide to methyl glycopyranoside acceptors Micromonospora viridifaciens

Organism

Organism UniProt Comment Textmining
Micromonospora viridifaciens Q02834
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Synonyms

Synonyms Comment Organism
neuraminidase
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Micromonospora viridifaciens
sialidase
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Micromonospora viridifaciens