Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties.

@article{Hong2006ProkaryoticTI,
  title={Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties.},
  author={Bum Soo Hong and Mi Kyung Yun and Yong-mei Zhang and Shigeru Chohnan and Charles O Rock and Stephen W. White and Suzanne Jackowski and Hee-won Park and Roberta Leonardi},
  journal={Structure},
  year={2006},
  volume={14 8},
  pages={1251-61}
}
Three distinct isoforms of pantothenate kinase (CoaA) in bacteria catalyze the first step in coenzyme A biosynthesis. The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties. PaCoaA has a fully enclosed pantothenate binding pocket and requires a monovalent cation to weakly bind ATP in an open cavity that… CONTINUE READING

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Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration

Zhang, Y.-M, C. O. Rock, S. Jackowski
J. Biol • 2006
View 3 Excerpts

The structure of the pantothenate kinase-ADP-pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator and antimetabolites

T. M. Laue, B. D. Shah, T. M. Ridgeway, S. L. Pelletier
J. Biol. Chem • 1992
View 1 Excerpt

A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

M. M. Bradford
Anal. Biochem • 1976
View 2 Excerpts

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