Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase

HIGHLIGHTS

  • who: Florence Vincent from the Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York , YW, United Kingdom have published the research work: Structure and Kinetics of a Monomeric Glucosamine 6-Phosphate Deaminase, in the Journal: (JOURNAL) of February/24,/2005

SUMMARY

    To reach the ligand-free T-state, the enzyme needs to bind the allosteric_activator GlcNAc-6-P. The lack of multimers and the absence of an activator-binding_site suggest that BsuNagB is not regulated by an allosteric mechanism. The exact cause of substrate inhibition is not known; most likely, a . . .

     

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