The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Two‐Metal Ion Catalysis in Enzymatic Acyl‐ and Phosphoryl‐Transfer Reactions
Abstract
Numerous studies, both in enzymatic and nonenzymatic catalysis, have been undertaken to understand the way by which metal ions, especially zinc ions, promote the hydrolysis of phosphate ester and amide bonds. Hydrolases containing one metal ion in the active site, termed mononuclear metallohydrolases, such as carboxypeptidase. A and thermolysin were among the first enzymes to have their structures unraveled by X‐ray crystallography. In recent years an increasing number of metalloenzymes have been identified that use two or more adjacent metal ions in the catalysis of phosphoryl‐transfer reactions (R‐OPO 3 + R′‐OH → R′‐OPO 3 + R‐OH; in the case of the phosphatase reaction R′‐OH is a water molecule) and carbonyl‐transfer reactions, for example, in peptidases or other amidases. These dinuclear metalloenzymes catalyze a great variety of these reactions, including hydrolytic cleavage of phosphomono‐, ‐di‐ and ‐triester bonds, phosphoanhydride bonds as well as of peptide bonds or urea. In addition, the formation of the phosphodiester bond of RNA and DNA by polymerases is catalyzed by a two‐metal ion mechanism. A remarkable diversity is also seen in the structures of the active sites of these di‐ and trinuclear metalloenzymes, even for enzymes that catalyze very similar reactions. The determination of the structure of a substrate, product, stable intermediate, or a reaction coordinate analogue compound bound to an active or inactivated enzyme is a powerful approach to investigate mechanistic details of enzyme action. Such studies have been applied to several of the metalloenzymes reviewed in this article; together with many other biochemical studies they provide a growing body of information on how the two (or more) metal ions cooperate to achieve efficient catalysis.
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Cites
Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA Polymerase
Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., & Erlich, H. A. (1988) · Science · doi:10.1126/science.2448875 · Cited by 17,719
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684
Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914
A general two-metal-ion mechanism for catalytic RNA
Steitz, T. A., & Steitz, J. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6498 · Cited by 1,171
Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810
Origins and evolutionary relationships of retroviruses
Doolittle, R. F., Johnson, M. S., & McClure, M. A. (1989) · The Quarterly Review of Biology · doi:10.1086/416128 · Cited by 577
Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
Davies, J. F., Hostomska, Z., Hostomsky, Z., Jordan, S. R., & Matthews, D. A. (1991) · Science · doi:10.1126/science.1707186 · Cited by 570
Johnson, M. S., McClure, M. A., Feng, D. F., Gray, J., & Doolittle, R. F. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.20.7648 · Cited by 480
Biochemical Basis of DNA Replication Fidelity
Goodman, M. F., Creighton, S., Bloom, L. B., Petruska, J., & Kunkel, T. A. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309086792 · Cited by 446
Three-dimensional structure of ribonuclease H from E. coli
Katayanagi, K., Miyagawa, M., Matsushima, M., Ishikawa, M., Kanaya, S., Ikehara, M., Matsuzaki, T., & Morikawa, K. (1990) · Nature · doi:10.1038/347306a0 · Cited by 349
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Structures and mechanisms of Nudix hydrolases
Mildvan, A. S., Xia, Z., Azurmendi, H. F., Saraswat, V., Legler, P. M., Massiah, M. A., Gabelli, S. B., Bianchet, M. A., Kang, L.-W., & Amzel, L. M. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.08.017 · Cited by 314
Crystal Structure of the Catalytic Core of an RNA-Polymerase Ribozyme
Shechner, D. M., Grant, R. A., Bagby, S. C., Koldobskaya, Y., Piccirilli, J. A., & Bartel, D. P. (2009) · Science · doi:10.1126/science.1174676 · Cited by 136
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Metadata
- Authors
- Sträter, N., Lipscomb, W. N., Klabunde, T., & Krebs, B.
- Venue
- Angewandte Chemie International Edition in English
- Publisher
- Wiley
- Published
- 1996-10
- Volume
- 35
- Issue
- 18
- Pages
- 2024-2055
- ISSN
- 0570-0833 (ISSN-L)
- OpenAlex
- W1994103683
- Cited by
- 611
- References
- 14
- FWCI
- 25.43
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sträter, N., Lipscomb, W. N., Klabunde, T., & Krebs, B. (1996). Two‐Metal Ion Catalysis in Enzymatic Acyl‐ and Phosphoryl‐Transfer Reactions. Angewandte Chemie International Edition in English. https://doi.org/10.1002/anie.199620241
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