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Gene Review

panB  -  3-methyl-2-oxobutanoate...

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs0138


High impact information on ECs0138


Chemical compound and disease context of ECs0138


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


  1. Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. Powers, S.G., Snell, E.E. J. Biol. Chem. (1976) [Pubmed]
  2. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. Teller, J.H., Powers, S.G., Snell, E.E. J. Biol. Chem. (1976) [Pubmed]
  3. 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]
  4. 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]
  5. 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]
  6. 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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