A computer modelling approach to study the mode of binding of L-lyxoflavin-5'-monophosphate to flavodoxin.
The mode of binding of L-lyxoflavin-5'-monophosphate has been studied by a computer modelling method. Energetically preferred conformers of L-lyxoflavin-5'-monophosphate have been obtained using empirical potential energy functions. These minimum energy conformers were used to study the mode of their binding to flavodoxin. The study indicates that L-lyxoflavin-5'-monophosphate can also have coenzymatic activity similar to flavin mononucleotide. But its lower activity compared to flavin mononucleotide is due to the lower conformer population that initiates the binding process. It is also concluded from this study that the inability of L-lyxoflavin to promote growth in some cases is at the phosphorylation level and not at the coenzyme level.
Vinayaka
C R
CR
Molecular Biophysics Unit, Indian Institute of Science, Bangalore.
Rao
V S
VS
D003067:Coenzymes / Q000378:metabolism; D003198:Computer Simulation; D005415:Flavins / Q000378:metabolism*; D005418:Flavodoxin / Q000378:metabolism*; D005420:Flavoproteins / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation; D013329:Structure-Activity Relationship; D013403:Sugar Phosphates / Q000378:metabolism*
D003067:Coenzymes; D005415:Flavins; D005418:Flavodoxin; D005420:Flavoproteins; D013403:Sugar Phosphates; C062478:lyxoflavin 5'-monophosphate