The DOI matches its Crossref record.
A Specific, Highly Active Malate Dehydrogenase by Redesign of a Lactate Dehydrogenase Framework
Abstract
Three variations to the structure of the nicotinamide adenine dinucleotide (NAD)-dependent L-lactate dehydrogenase from Bacillus stearothermophilus were made to try to change the substrate specificity from lactate to malate: Asp 197 → Asn, Thr 246 → Gly, and Gln 102 → Arg). Each modification shifts the specificity from lactate to malate, although only the last (Gln 102 → Arg) provides an effective and highly specific catalyst for the new substrate. This synthetic enzyme has a ratio of catalytic rate ( k cat ) to Michaelis constant ( K m ) for oxaloacetate of 4.2 x 10 6 M -1 s -1 , equal to that of native lactate dehydrogenase for its natural substrate, pyruvate, and a maximum velocity (250 s -1 ), which is double that reported for a natural malate dehydrogenase from B. stearothermophilus .
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Citations
Cited by
L-2-Hydroxyglutarate production arises from noncanonical enzyme function at acidic pH
Intlekofer, A. M., Wang, B., Liu, H., Shah, H., Carmona-Fontaine, C., Rustenburg, A. S., Salah, S., Gunner, M. R., Chodera, J. D., Cross, J. R., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2307 · Cited by 268
Pollack, J. D., Williams, M. V., & McElhaney, R. N. (1997) · Critical Reviews in Microbiology · doi:10.3109/10408419709115140 · Cited by 180
Hofhuis, J., Schueren, F., Nötzel, C., Lingner, T., Gärtner, J., Jahn, O., & Thoms, S. (2016) · Open Biology · doi:10.1098/rsob.160246 · Cited by 59
Malate/lactate dehydrogenase in mollicutes: evidence for a multienzyme protein
Cordwell, S. J., Basseal, D. J., Pollack, J. D., & Humphery-Smith, I. (1997) · Gene · doi:10.1016/s0378-1119(97)00063-2 · Cited by 42
Metadata
- Authors
- Wilks, H. M., Hart, K. W., Feeney, R., Dunn, C. R., Muirhead, H., Chia, W. N., Barstow, D. A., Atkinson, T., Clarke, A. R., & Holbrook, J. J.
- Venue
- Science
- Published
- 1988-12-16
- Volume
- 242
- Issue
- 4885
- Pages
- 1541-1544
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2062880866
- Cited by
- 276
- References
- 0
- FWCI
- 4.07
- Type
- journal article
- Language
- en
- Open access
- closed
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