N-acetyl-D-neuraminic acid lyase generates the sialic acid for colominic acid biosynthesis in Escherichia coli K1.

@article{Ferrero1996NacetylDneuraminicAL,
  title={N-acetyl-D-neuraminic acid lyase generates the sialic acid for colominic acid biosynthesis in Escherichia coli K1.},
  author={M. A. Ferrero and {\'A}. Reglero and M. Fernandez-Lopez and R. Ordas and L. Rodr{\'i}guez-Aparicio},
  journal={The Biochemical journal},
  year={1996},
  volume={317 ( Pt 1)},
  pages={
          157-65
        }
}
Colominic acid is a capsular homopolymer from Escherichia coli K1 composed of alpha (2-8)-linked N-acetyl-D-neuraminic acid (NeuAc) residues. Recently, we have described that NeuAc synthesis in this bacterium occurs through the action of NeuAc lyase (EC 4.1.3.3) [ Rodríguez-Aparicio, Ferrero and Reglero (1995) Biochem. J.308, 501-505]. In the present work we analysed and characterized this enzyme. E. coli K1 NeuAc lyase is detected from the early logarithmic phase of growth, is induced by NeuAc… Expand
Purification and characterization of N-acetylneuraminic acid-9-phosphate synthase from rat liver.
TLDR
Rat Neu5Ac-9-phosphate synthase was purified 11,700-fold from rat liver cytosol to apparent homogeneity by ammonium sulfate precipitation, chromatography on hydroxylapatite, phenyl-Sepharose, MonoQ, and finally gel filtration, indicating that the enzyme is a dimer composed of 37-kDa subunits. Expand
Purification and characterization of GlcNAc-6-P 2-epimerase from Escherichia coli K92.
TLDR
The results indicate that, unlike UDP-GlcNAc 2-epimerase, which promotes the biosynthesis of sialic acid, Glc NAc-6-P 2-EPimerase plays a catabolic role. Expand
Structural basis for substrate specificity and mechanism of N-acetyl-D-neuraminic acid lyase from Pasteurella multocida.
TLDR
The crystal structures of wild-type Pasteurella multocida N-acetylneuraminate lyase and its K164A mutant reveal that every hydroxyl group of the linear sugars makes hydrogen bond interactions with the enzyme, and the residues that determine specificity were identified. Expand
Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: insights into the reaction mechanism.
TLDR
The N-acetylneuraminate lyase from Clostridium perfringens was expressed in Escherichia coli as a fusion protein with a His-tag and purified to homogeneity using metal chelate affinity and anion exchange chromatography and a model of the reaction mechanism is discussed. Expand
Pasteurella multocida sialic acid aldolase: a promising biocatalyst
TLDR
Substrates specificity studies showed that 5-O-methyl-ManNAc, a ManNAc derivative, can be used efficiently as a substrate by PmNanA, but not efficiently by EcNAnA, for the synthesis of 8- O-methyl Neu5Ac. Expand
Characterization of a novel N-acetylneuraminate lyase from Staphylococcus carnosus TM300 and its application to N-acetylneuraminic acid production.
The possibility of incorporating N-acetylneuraminic acid (Neu5Ac) in infant formulas and other functional foods has opened up the need to synthesize N-acetylneuraminic acid using N-acetylneuraminateExpand
Production of N-acetyl-d-neuraminic Acid by Recombinant Single Whole Cells Co-expressing N-acetyl-d-glucosamine-2-epimerase and N-acetyl-d-neuraminic Acid Aldolase
TLDR
It is demonstrated that using recombinant E. coli cells synchronously expressing bAGE and NanA as biocatalysts could potentially be used in the industrial mass production of Neu5Ac. Expand
Determination of different amino sugar 2'-epimerase activities by coupling to N-acetylneuraminate synthesis.
TLDR
This system provides a sensitive, rapid, reproducible, specific and simple procedure (feasible with commercial reagents) for measuring amino sugar 2'-epimerases from eukaryotic and prokaryotic sources. Expand
N‐Acetylneuraminic acid uptake in Pasteurella (Mannheimia) haemolytica A2 occurs by an inducible and specific transport system
TLDR
The N‐acetylneuraminic acid (NeuAc) transport system of Pasteurella (Mannheimia) haemolytica A2 was studied and the notion that NeuAc uptake is an active sugar cation symporter is supported. Expand
Transport of N-acetyl-D-galactosamine in Escherichia coli K92: effect on acetyl-amino sugar metabolism and polysialic acid production.
TLDR
Results strongly support the notion that GalNAc uptake depends on a specific phosphotransferase system and show that E. coli K92 has developed a regulation mechanism that specifically induces the appropriate permease based on the presence of each respective phospho-amino sugar. Expand
...
1
2
3
4
...

References

Molecular cloning of the K1 capsular polysaccharide genes of E. coli
TLDR
Recombinant DNA methodology provides a powerful tool for studying whether the K1 antigen is sufficient to confer virulence or if other E. coli structures are necessary, and cloned K1 genes synthesize a capsule in E.E. coli K12 indistinguishable chemically and immunologically from that of wild-type K1 strains. Expand