Disease relevance of L-pantoate

• Purification of pantoate and dimethylmalate dehydrogenase from Pseudomonas fluorescens UK-1 [1].

High impact information on L-pantoate

• Our data suggest that specific subunit contacts were selected and maintained in the plant lineage of the pantothenate synthetase protein family and that the resulting allosteric interactions are balanced for efficient catalysis at low pantoate levels [2].
• A new crystal form was also obtained; it displays the flexible wall of the active site cavity in a conformation incapable of binding pantoate [3].
• Ketopantoate reductase (KPR, EC 1.1.1.169) catalyzes the NADPH-dependent reduction of ketopantoate to pantoate on the pantothenate (vitamin B(5)) biosynthetic pathway [4].
• Effect of 2,4,6-trinitrobenzenesulfonic acid and pyridoxal 5'-phosphate on pantoate dehydrogenase from Pseudomonas fluorescens UK-1 [5].
• Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase [6].

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].

References