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Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin evidence for substrate assisted catalysis
Open accessAbstract
The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 A resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at C1 is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2.
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Cites
Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta
Kramer, K. J., Corpuz, L., Choi, H. K., & Muthukrishnan, S. (1993) · Insect Biochemistry and Molecular Biology · doi:10.1016/0965-1748(93)90043-r · Cited by 213
Morgavi, D. P., Sakurada, M., Tomita, Y., & Onodera, R. (1994) · Microbiology · doi:10.1099/00221287-140-3-631 · Cited by 47
Cited by
Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases
Merzendorfer, H., & Zimoch, L. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00709 · Cited by 1,250
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717
Rye, C. S., & Withers, S. G. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00135-6 · Cited by 470
The molecular biology of chitin digestion
Cohen-Kupiec, R., & Chet, I. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80058-x · Cited by 334
Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-Å resolution
van Aalten, D. M. F., Synstad, B., Brurberg, M. B., Hough, E., Riise, B. W., Eijsink, V. G. H., & Wierenga, R. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.5842 · Cited by 265
Metadata
- Authors
- Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., & Dijkstra, B. W.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-12-05
- Volume
- 34
- Issue
- 48
- Pages
- 15619-15623
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2266642515
- Cited by
- 346
- References
- 2
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- green
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- Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., & Dijkstra, B. W. (1995). Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin evidence for substrate assisted catalysis. Biochemistry. https://doi.org/10.1021/bi00048a003
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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