EC 1.1.1.367 - UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase

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IntEnz Enzyme Nomenclature
EC 1.1.1.367

Names

Accepted name:
UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase
Other names:
WbjC
Cap5F
Systematic name:
UDP-2-acetamido-2,6-dideoxy-L-talose:NADP+ oxidoreductase

Reactions

Comments:

Part of the biosynthesis of UDP-N-acetyl-L-fucosamine. Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Kneidinger, B., O'Riordan, K., Li, J., Brisson, J. R., Lee, J. C., Lam, J. S.
    Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway.
    J. Biol. Chem. 278 : 3615-3627 (2003). [PMID: 12464616]
  2. Mulrooney, E. F., Poon, K. K., McNally, D. J., Brisson, J. R., Lam, J. S.
    Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11.
    J. Biol. Chem. 280 : 19535-19542 (2005). [PMID: 15778500]
  3. Miyafusa, T., Tanaka, Y., Kuroda, M., Ohta, T., Tsumoto, K.
    Expression, purification, crystallization and preliminary diffraction analysis of CapF, a capsular polysaccharide-synthesis enzyme from Staphylococcus aureus.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 : 512-515 (2008). [PMID: 18540063]

[EC 1.1.1.367 created 2014]