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Gene Review:

panB - 3-methyl-2-oxobutanoate...

Escherichia coli O157:H7 str. Sakai

Schmitzberger, F. et al., Teller, J.H. et al., Ottenhof, H.H. et al., von Delft, F. et al., Jones, C.E. et al., et al.

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Disease relevance of ECs0138

Some physical, catalytic, and regulatory properties of ketopantoate hydroxymethyltransferase (5,10-methylenetetrahydrofolate: alpha-ketoisovalerate hydroxymethyltranferase) from Escherichia coli are described [1].

High impact information on ECs0138

Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis [2].
A new enzyme, ketopantoate hydroxymethyltransferase (5,10-methylene tetrahydrofolate: alpha-ketoisovalerate hydroxymethyltransferase) has been purified 2400-fold to apparent homogeneity from Escherichia coli K12 [2].
KPHMT enzyme activity could be measured in purified mitochondria from both pea leaves and Arabidopsis suspension cultures [3].
Two genes encoding KPHMT and one for PtS were identified in the Arabidopsis thaliana genome, and cDNAs for all three genes were amplified by PCR [3].
We show that KPHMT forms a family within the phosphoenolpyruvate/pyruvate superfamily [4].

Chemical compound and disease context of ECs0138

Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily [4].
Escherichia coli ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first step in the biosynthesis pathway of pantothenate (vitamin B(5)), the transfer of a hydroxymethyl group onto alpha-ketoisovalerate [4].
We report the crystal structure of E. coli ketopantoate hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its product, ketopantoate [5].

Biological context of ECs0138

Here we describe a detailed comparative analysis of the KPHMT crystal structure and the identification of structural homologues, some of which have remarkable similarities in their active sites, modes of binding to substrates, and mechanisms [4].
The identity of the gene product as ketopantoate hydroxymethyltransferase was confirmed by purification of the enzyme protein, which was overexpressed approximately 50-fold in the mutant harboring the gene on a high-copy-number plasmid [6].

Associations of ECs0138 with chemical compounds

KPHMT adopts the (betaalpha)(8) barrel fold and is a member of the phosphoenolpyruvate/pyruvate superfamily [5].

References

Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. Powers, S.G., Snell, E.E. J. Biol. Chem. (1976) [Pubmed]
Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. Teller, J.H., Powers, S.G., Snell, E.E. J. Biol. Chem. (1976) [Pubmed]
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]
Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily. Schmitzberger, F., Smith, A.G., Abell, C., Blundell, T.L. J. Bacteriol. (2003) [Pubmed]
Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. von Delft, F., Inoue, T., Saldanha, S.A., Ottenhof, H.H., Schmitzberger, F., Birch, L.M., Dhanaraj, V., Witty, M., Smith, A.G., Blundell, T.L., Abell, C. Structure (Camb.) (2003) [Pubmed]
Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme. Jones, C.E., Brook, J.M., Buck, D., Abell, C., Smith, A.G. J. Bacteriol. (1993) [Pubmed]

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