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Chemical Compound Review: 

melibiose     6-[[3,4,5-trihydroxy-6- (hydroxymethyl)oxan...

 
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Disease relevance of melibiose

 

High impact information on melibiose

  • The resulting restricted access to the intermediate helps to explain why allolactose, the natural inducer for the lac operon, is the preferred product of transglycosylation [2].
  • The transfer products from galactosyl-ebgabcd and galactosyl-ebgabcde to high concentrations to glucose have been measured; the predominant product is allolactose, but significant quantities of lactose are also formed; however, at apparent kinetic saturation of the galactosyl-enzyme, hydrolysis rather than transfer is the preponderant pathway [3].
 

Associations of melibiose with other chemical compounds

 

Gene context of melibiose

References

  1. Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer. Huber, R.E., Hakda, S., Cheng, C., Cupples, C.G., Edwards, R.A. Biochemistry (2003)
  2. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Juers, D.H., Heightman, T.D., Vasella, A., McCarter, J.D., Mackenzie, L., Withers, S.G., Matthews, B.W. Biochemistry (2001)
  3. Catalytic consequences of experimental evolution: catalysis by a 'third-generation' evolvant of the second beta-galactosidase of Escherichia coli, ebgabcde, and by ebgabcd, a 'second-generation' evolvant containing two supposedly 'kinetically silent' mutations. Krishnan, S., Hall, B.G., Sinnott, M.L. Biochem. J. (1995)
  4. Transgalactosylation activity of ebg beta-galactosidase synthesizes allolactose from lactose. Hall, B.G. J. Bacteriol. (1982)
  5. Reversion reactions of beta-galactosidase (Escherichia coli). Huber, R.E., Hurlburt, K.L. Arch. Biochem. Biophys. (1986)
  6. The action of beta-galactosidase (Escherichia coli) on allolactose. Huber, R.E., Wallenfels, K., Kurz, G. Can. J. Biochem. (1975)
 
 
 
 
 
 
 
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