Allolactose

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&nbsp;Allolactose is a molecule made of galactose and glucose joined by alpha - 1,6 glycosidic bond. It is the side product of the conversion of lactose to galactose and glucose by beta- galactosidase. Allolactose is an inducer of lac operon in prokaryotes. It binds to the lac repressor causing a comformational change which reduces the reprossor's affinity for the operator DNA. As results RNA polymerase can initiate transcription of the lac genes.<ref>Berg JM, Tymoczko JL, Gatto GJ, Stryer L. Biochemistry. 8th ed. New York: W.H. Freeman &amp;amp; Commpany, a Macmillan Education Print. 2015</ref>  
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&nbsp;Allolactose is a molecule made of galactose and glucose joined by alpha - 1,6 [https://teaching.ncl.ac.uk/bms/wiki/index.php/Glycosidic_bond glycosidic bond]. It is the side product of the conversion of lactose to galactose and glucose by beta- galactosidase. Allolactose is an inducer of [https://teaching.ncl.ac.uk/bms/wiki/index.php/Lac_operon lac operon] in prokaryotes. It binds to the lac repressor causing a comformational change which reduces the reprossor's affinity for the operator DNA. As results [https://teaching.ncl.ac.uk/bms/wiki/index.php/RNA_polymerase RNA polymerase] can initiate transcription of the lac genes.<ref>Berg JM, Tymoczko JL, Gatto GJ, Stryer L. Biochemistry. 8th ed. New York: W.H. Freeman &amp;amp;amp; Commpany, a Macmillan Education Print. 2015</ref>  
  
 
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Revision as of 17:15, 4 December 2017

 Allolactose is a molecule made of galactose and glucose joined by alpha - 1,6 glycosidic bond. It is the side product of the conversion of lactose to galactose and glucose by beta- galactosidase. Allolactose is an inducer of lac operon in prokaryotes. It binds to the lac repressor causing a comformational change which reduces the reprossor's affinity for the operator DNA. As results RNA polymerase can initiate transcription of the lac genes.[1]


References

  1. Berg JM, Tymoczko JL, Gatto GJ, Stryer L. Biochemistry. 8th ed. New York: W.H. Freeman &amp;amp; Commpany, a Macmillan Education Print. 2015
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