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Chemical Compound Review

AG-F-60484     2,4-dihydroxy-3,3-dimethyl- butanoic acid

Synonyms: CHEBI:14737, AC1Q5SPZ, CTK4I9678, AR-1D3621, AKOS006378212, ...
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Disease relevance of L-pantoate


High impact information on L-pantoate


Associations of L-pantoate with other chemical compounds

  • Thus, interactions between the pantoic acid domain of CoA and the active site destabilize E-CoA by approximately 4.8 kcal/mol, approximately 1.3 kcal/mol of which arises from interaction with the amide group of the pantoic acid domain and approximately 3.5 kcal/mol of which arises from interaction with other portions of the pantoic acid domain [7].

Gene context of L-pantoate

  • The apparent equilibrium constant, K(eq)', of 676 at pH 7.5 and the standard free energy change, DeltaG, of -14 kcal/mol suggest that ketopantoate reductase reaction is very favorable in the physiologically important direction of pantoate formation [8].


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  2. Molecular adaptation and allostery in plant pantothenate synthetases. Jonczyk, R., Genschel, U. J. Biol. Chem. (2006) [Pubmed]
  3. Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in action. Wang, S., Eisenberg, D. Biochemistry (2006) [Pubmed]
  4. Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism. Matak-Vinković, D., Vinković, M., Saldanha, S.A., Ashurst, J.L., von Delft, F., Inoue, T., Miguel, R.N., Smith, A.G., Blundell, T.L., Abell, C. Biochemistry (2001) [Pubmed]
  5. Effect of 2,4,6-trinitrobenzenesulfonic acid and pyridoxal 5'-phosphate on pantoate dehydrogenase from Pseudomonas fluorescens UK-1. Mäntsälä, P. Acta Chem. Scand., B, Org. Chem. Biochem. (1980) [Pubmed]
  6. Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase. Myöhänen, T., Mäntsälä, P. Biochim. Biophys. Acta (1980) [Pubmed]
  7. Role of binding energy with coenzyme A in catalysis by 3-oxoacid coenzyme A transferase. Whitty, A., Fierke, C.A., Jencks, W.P. Biochemistry (1995) [Pubmed]
  8. Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase. Zheng, R., Blanchard, J.S. Biochemistry (2000) [Pubmed]
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