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Chemical Compound Review:

AC1O43P9 (2R,4R,5R,6R)-2,4,5- trihydroxy-6-(1...

Synonyms:

Brabetz, W. et al., Asojo, O. et al., Vainer, R. et al., Shulami, S. et al.

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Disease relevance of (2R,4R,5R,6R)-2,4,5-trihydroxy-6-(1-hydroxy-2-phosphonooxy-ethyl)tetrahydropyran-2-carboxylic acid

A reciprocal single mutation affects the metal requirement of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthases from Aquifex pyrophilus and Escherichia coli [1].
Molecular cloning, sequence analysis and functional characterization of the gene kdsA, encoding 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase of Chlamydia psittaci 6BC [2].
The kdsA gene encoding 3-deoxy-D-manno-2-octulosonate-8-phosphate (Kdo-8-P) synthase of Chlamydia psittaci 6BC was cloned by complementing the temperature-sensitive kdsA mutant Salmonella enterica serovar Typhimurium AG701i50 [2].

High impact information on (2R,4R,5R,6R)-2,4,5-trihydroxy-6-(1-hydroxy-2-phosphonooxy-ethyl)tetrahydropyran-2-carboxylic acid

The enzyme 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase (KDO8PS) catalyses the condensation of arabinose 5-phosphate (A5P) and phosphoenol pyruvate (PEP) to obtain 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) [3].
The crystal structures of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase (KDOPS) from Escherichia coli complexed with the substrate phosphoenolpyruvate (PEP) and with a mechanism-based inhibitor (K(d) = 0.4 microM) were determined by molecular replacement using X-ray diffraction data to 2.8 and 2.3 A resolution, respectively [4].

References

A reciprocal single mutation affects the metal requirement of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthases from Aquifex pyrophilus and Escherichia coli. Shulami, S., Furdui, C., Adir, N., Shoham, Y., Anderson, K.S., Baasov, T. J. Biol. Chem. (2004) [Pubmed]
Molecular cloning, sequence analysis and functional characterization of the gene kdsA, encoding 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase of Chlamydia psittaci 6BC. Brabetz, W., Brade, H. Eur. J. Biochem. (1997) [Pubmed]
Crystal structures of Escherichia coli KDO8P synthase complexes reveal the source of catalytic irreversibility. Vainer, R., Belakhov, V., Rabkin, E., Baasov, T., Adir, N. J. Mol. Biol. (2005) [Pubmed]
Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor. Asojo, O., Friedman, J., Adir, N., Belakhov, V., Shoham, Y., Baasov, T. Biochemistry (2001) [Pubmed]

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