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Gene Review:

ECs0479 - 2-dehydropantoate 2-reductase

Escherichia coli O157:H7 str. Sakai

Zheng, R. et al., Matak-Vinković, D. et al., Zheng, R. et al., Ottenhof, H.H. et al., Elischewski, F. et al., et al.

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Disease relevance of ECs0479

We investigated whether Arabidopsis encoded homologues of the remaining two pantothenate biosynthesis enzymes from E. coli, l-aspartate-alpha-decarboxylase (ADC) and ketopantoate reductase (KPR) [1].
We show here that the Corynebacterium glutamicum ilvC gene is able to complement a ketopantoate reductase deficient Escherichia coli mutant [2].

High impact information on ECs0479

The NADPH-dependent reduction of ketopantoate to pantoate, catalyzed by ketopantoate reductase (KPR; EC 1.1.1.169), is essential for the biosynthesis of pantothenate (vitamin B(5)) [3].
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound [3].
Substrate specificity and kinetic isotope effect analysis of the Eschericia coli ketopantoate reductase [4].
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 [5].
The structure of KPR was determined by the multiwavelength anomalous dispersion method using the SeMet protein, for which data were collected to 2.3 A resolution [5].

Chemical compound and disease context of ECs0479

These results indicate that Lys176 and Glu256 of the E. coli ketopantoate reductase are active site residues, and we propose specific roles for each in binding ketopantoate and catalysis [6].
The Escherichia coli panE gene encoding KPR was cloned and expressed at high levels as the native and selenomethionine-substituted (SeMet) proteins [5].
Pantothenate production in Escherichia coli K12 by enhanced expression of the panE gene encoding ketopantoate reductase [7].

Biological context of ECs0479

Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue [6].

Associations of ECs0479 with chemical compounds

Ketopantoate reductase (EC 1.1.1.169) catalyzes the NADPH-dependent reduction of alpha-ketopantoate to D-(-)-pantoate in the biosynthesis of pantothenate [6].
Ketopantoate reductase (EC 1.1.1.169), an enzyme in the pantothenate biosynthetic pathway, catalyzes the NADPH-dependent reduction of alpha-ketopantoate to form D-(-)-pantoate [4].
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].
Ketopantoate reductase (EC 1.1.1.169) catalyzes the NADPH-dependent reduction of alpha-ketopantoate to form D-(-)-pantoate in the pantothenate/coenzyme A biosynthetic pathway [8].
Ketopantoate reductase catalyzes the second step of the pantothenate pathway after ketoisovalerate, common intermediate in valine, leucine and pantothenate biosynthesis [2].

References

Organisation of the pantothenate (vitamin B5) biosynthesis pathway in higher plants. Ottenhof, H.H., Ashurst, J.L., Whitney, H.M., Saldanha, S.A., Schmitzberger, F., Gweon, H.S., Blundell, T.L., Abell, C., Smith, A.G. Plant J. (2004) [Pubmed]
Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum. Merkamm, M., Chassagnole, C., Lindley, N.D., Guyonvarch, A. J. Biotechnol. (2003) [Pubmed]
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. Lobley, C.M., Ciulli, A., Whitney, H.M., Williams, G., Smith, A.G., Abell, C., Blundell, T.L. Biochemistry (2005) [Pubmed]
Substrate specificity and kinetic isotope effect analysis of the Eschericia coli ketopantoate reductase. Zheng, R., Blanchard, J.S. Biochemistry (2003) [Pubmed]
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]
Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue. Zheng, R., Blanchard, J.S. Biochemistry (2000) [Pubmed]
Pantothenate production in Escherichia coli K12 by enhanced expression of the panE gene encoding ketopantoate reductase. Elischewski, F., Pühler, A., Kalinowski, J. J. Biotechnol. (1999) [Pubmed]
Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase. Zheng, R., Blanchard, J.S. Biochemistry (2000) [Pubmed]

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