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Literature summary for 4.2.1.135 extracted from

  • Morrison, J.P.; Troutman, J.M.; Imperiali, B.
    Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway (2010), Bioorg. Med. Chem., 18, 8167-8171.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.135

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100 at 0.04% 30fold higher activity than at 1% Campylobacter jejuni

Application

Application Comment Organism
biotechnology assay targets enzymes involved in the biosynthesis of the unusual bacterial sugar diNAcBac and the transfer of diNAcBac-phosphate to UndP. This multienzyme assay, together with the established assays for the individual enzymes, can be used to screen for inhibitors, and may be used to evaluate substrate flux along the inhibited pathway. This assay is optimized for maximum sensitivity to inhibition of PglF, PglE, PglD, and PglC by balancing the enzyme concentrations such that each is partially rate determining Campylobacter jejuni

Cloned(Commentary)

Cloned (Comment) Organism
recombinantly expressed Campylobacter jejuni

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using affinity chromatography Campylobacter jejuni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetylglucosamine
-
 Campylobacter jejuni ?
-
 ?

Synonyms

Synonyms Comment Organism
PglF
-
 Campylobacter jejuni

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Campylobacter jejuni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Campylobacter jejuni