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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Chemical Compound Review: 

arabinose-5P     [(2R,3R,4S)-2,3,4-trihydroxy- 5-oxo...

Synonyms: D-A-5-P, CHEMBL1162524, CHEBI:16241, HMDB11734, AC1L4MLG, ...
 
 
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Disease relevance of D-A-5-P

  • The results reveal the si face addition of the PEP to the re face of the carbonyl of A5P, and establish that the stereochemistry of ApKDO8PS is identical to that of the metal-independent Escherichia coli KDO8P synthase enzyme (EcKDO8PS) [1].
 

High impact information on D-A-5-P

  • Arabinose 5-phosphate isomerase (API), encoded by Y. pestis yrbH, catalyses the conversion of ribulose 5-phosphate into arabinose 5-phosphate (A5P), the first committed step in the 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) biosynthesis pathway [2].
  • The X-ray structure of the wild-type enzyme shows that when both PEP and A5P bind, the active site becomes isolated from the environment due to a conformational change of the L7 loop [3].

References

  1. The use of (E)- and (Z)-phosphoenol-3-fluoropyruvate as mechanistic probes reveals significant differences between the active sites of KDO8P and DAHP synthases. Furdui, C.M., Sau, A.K., Yaniv, O., Belakhov, V., Woodard, R.W., Baasov, T., Anderson, K.S. Biochemistry (2005) [Pubmed]
  2. Yersinia pestis YrbH is a multifunctional protein required for both 3-deoxy-D-manno-oct-2-ulosonic acid biosynthesis and biofilm formation. Tan, L., Darby, C. Mol. Microbiol. (2006) [Pubmed]
  3. The catalytic and conformational cycle of Aquifex aeolicus KDO8P synthase: role of the L7 loop. Xu, X., Kona, F., Wang, J., Lu, J., Stemmler, T., Gatti, D.L. Biochemistry (2005) [Pubmed]
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