The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature
Open accessAbstract
Short‐chain dehydrogenases/reductases (SDR) and medium‐chain dehydrogenases/reductases (MDR) are protein families originally distinguished from characterisations of alcohol dehydrogenase of these two types. Screening of completed genome sequences now reveals that both these families are large, wide‐spread and complex. In Escherichia coli alone, there are no fewer than 17 MDR forms, identified as open reading frames, considerably extending previously known MDR relationships in prokaryotes and including ethanol‐active alcohol dehydrogenase. In entire databanks, 1056 SDR and 537 MDR forms are currently known, extending the multiplicity further. Complexity is also large, with several enzyme activity types, subgroups and evolutionary patterns. Repeated duplications can be traced for the alcohol dehydrogenases, with independent enzymogenesis of ethanol activity, showing a general importance of this enzyme activity.
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Citations
Cites
Improved tools for biological sequence comparison.
Pearson, W. R., & Lipman, D. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.8.2444 · Cited by 11,227
Cited by
Kavanagh, K. L., Jörnvall, H., Persson, B., & Oppermann, U. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8588-y · Cited by 908
Self-citationCheng, W.-H., Endo, A., Zhou, L., Penney, J., Chen, H.-C., Arroyo, A., Leon, P., Nambara, E., Asami, T., Seo, M., et al. (2002) · The Plant Cell · doi:10.1105/tpc.006494 · Cited by 871
Kallberg, Y., Oppermann, U., Jörnvall, H., & Persson, B. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03130.x · Cited by 430
Self-citationThe SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative
Persson, B., Kallberg, Y., Bray, J. E., Bruford, E., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jörnvall, H., Kavanagh, K. L., Kedishvili, N., et al. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.040 · Cited by 396
Self-citationA Model of Structure and Catalysis for Ketoreductase Domains in Modular Polyketide Synthases
Reid, R., Piagentini, M., Rodriguez, E., Ashley, G., Viswanathan, N., Carney, J., Santi, D. V., Hutchinson, C. R., & McDaniel, R. (2003) · Biochemistry · doi:10.1021/bi0268706 · Cited by 310
Metadata
- Authors
- Jörnvall, H., Höög, J.-O., & Persson, B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-02-26
- Volume
- 445
- Issue
- 2-3
- Pages
- 261-264
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2020168271
- Cited by
- 198
- References
- 1
- FWCI
- 6.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Jörnvall, H., Höög, J.-O., & Persson, B. (1999). SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature. FEBS Letters. https://doi.org/10.1016/s0014-5793(99)00130-1
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