The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Catechol oxidase — structure and activity
Abstract
Recently determined structures of copper-containing plant catechol oxidase in three different catalytic states have provided new insights into the mechanism of this enzyme and its relationship to other copper type-3 proteins. Moreover, the active site of catechol oxidase has been found to be structurally conserved with the oxygen-binding site of a molluscan hemocyanin.
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Citations
Cites
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Cited by
The Crystal Structure of Catechol Oxidase: New Insight into the Function of Type-3 Copper Proteins
Gerdemann, C., Eicken, C., & Krebs, B. (2002) · Accounts of Chemical Research · doi:10.1021/ar990019a · Cited by 585
Self-citationSynthetic models of the active site of catechol oxidase: mechanistic studies
Koval, I. A., Gamez, P., Belle, C., Selmeczi, K., & Reedijk, J. (2006) · Chemical Society Reviews · doi:10.1039/b516250p · Cited by 527
Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
Decker, H., & Tuczek, F. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01602-9 · Cited by 377
First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity
Sendovski, M., Kanteev, M., Ben-Yosef, V. S., Adir, N., & Fishman, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.048 · Cited by 299
Metadata
- Authors
- Eicken, C., Krebs, B., & Sacchettini, J. C.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 9
- Issue
- 6
- Pages
- 677-683
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2019347060
- Cited by
- 259
- References
- 1
- FWCI
- 0.51
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
