M. tuberculosis Pantothenate Kinase: Dual Substrate Specificity and Unusual Changes in Ligand Locations

Kinetic measurements of enzyme activity indicate that type I pantothenate kinase from Mycobacterium tuberculosis has dual substrate specificity for ATP and GTP, unlike the enzyme from Escherichia coli, which shows a higher specificity for ATP. A molecular explanation for the difference in the specif...

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Veröffentlicht in:	Journal of molecular biology 2010-07, Vol.400 (2), p.171-185
Hauptverfasser:	Chetnani, Bhaskar, Kumar, Parimal, Surolia, A., Vijayan, M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino Acid Sequence Animals ATP ATP and GTP Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Catalytic Domain CoA biosynthesis pathway crystal structures Crystallography, X-Ray Escherichia coli Escherichia coli - enzymology Guanosine Diphosphate - chemistry Guanosine Diphosphate - metabolism Guanosine Triphosphate - analogs & derivatives Guanosine Triphosphate - chemistry Guanosine Triphosphate - metabolism Humans Ligands Models, Molecular Molecular Sequence Data Mycobacterium tuberculosis - enzymology Pantothenic Acid - chemistry Pantothenic Acid - metabolism Phosphotransferases (Alcohol Group Acceptor) - chemistry Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism productive and non-productive binding Protein Structure, Tertiary Substrate Specificity TB proteins
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