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Literature summary for 2.4.1.56 extracted from

  • Khaled, A.; Piotrowska, O.; Dominiak, K.; Auge, C.
    Exploring specificity of glycosyltransferases: synthesis of new sugar nucleotide related molecules as putative donor substrates (2008), Carbohydr. Res., 343, 167-178.
    View publication on PubMed
Search for more literature for 2.4.1.56

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Neisseria meningitidis

Inhibitors

Inhibitors Comment Organism Structure
2-acetamido-2-deoxy-alpha-D-glucopyranosyl 1-diphosphate
-
 Neisseria meningitidis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
 Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information synthesized donor substrates methyl-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-diphosphate, benzyl-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-diphosphate, 4-phenylbutyl-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-diphosphate and 2-acetamido-2-deoxy-alpha-D-glucopyranose 1-diphosphate show no reactivity Neisseria meningitidis ?
-
 ?
UDP-N-acetyl-D-glucosamine + beta-D-Galp-(1-4)-beta-D-Glcp-O-(CH2)6-NH-dansyl
-
 Neisseria meningitidis ?
-
 ?

Synonyms

Synonyms Comment Organism
LgtA
-
 Neisseria meningitidis
N-acetylglucosaminyltransferase
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Neisseria meningitidis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
7
-
-
 Neisseria meningitidis 2-acetamido-2-deoxy-alpha-D-glucopyranosyl 1-diphosphate