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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kirsch, Jack F. Yin, Yifeng |
| Description | Author Affiliation: Yin Y ( QB3 Institute, 572 Stanley Hall, University of California, Berkeley, CA 94720-3220, USA.); |
| Abstract | Five positions in the Escherichia coli malate dehydrogenase (eMDH) sequence, which distinguish MDH from lactate dehydrogenase (LDH) activity, were identified through a combination of Venn diagrams constructed from whole genomic data and from unbiased representative sequences from terminal clades. Incorporation of the five changes in eMDH sufficed to convert the enzyme from one with (k(cat)/K(m)(pyruvate))/(k(cat)/K(m)(oxaloacetate)) = 6.1 x 10(-9) to one with that ratio = 28. The substrate specificity was thus changed by a factor of 4.6 x 10(9). The k(cat)/K(m)(pyruvate) value for the pentamutant (eMDH I12V/R81Q/M85E/G210A/V214I) is 3,500 M(-1).s(-1), which is approximately equal 1/1,000 of the values found for typical wild-type LDHs. The procedure isolates an intersection of 'strong forcing sets' that should prove to be of general use in switching paralog function. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 44 |
| Volume Number | 104 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2007-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Enzymology Genetics L-Lactate Dehydrogenase Metabolism Malate Dehydrogenase Mutation Kinetics Chemistry Molecular Structure NAD Protein Binding Sensitivity And Specificity Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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