Abstract
Pectate lyases are depolymerizing enzymes that degrade plant cell walls, causing tissue maceration and death. The laboratory has been engaged in structural studies of several members of the pectate lyase superfamily. Most effort has been focused on Erwinia chrysanthemi pectate lyase C (PelC). There is now an accumulation of data that supports a detailed description of the enzymatic mechanism. The data include structural studies of native PelC, PelC-Ca2+ complexes, and an inactive PelC mutant complexed with an oligogalacturonic acid fragment. The structural studies have been supported by amino acid sequence alignments, site-specific mutagenesis experiments, kinetic studies at various pHs, and deuterium labeling studies. Together, the data implicate an invariant arginine as the amino acid that initiates proton abstraction in the β-elimination cleavage of pectate. The data suggest several potential sources of the proton donated to the scissile glycosidic bond to complete the reaction, but do not provide sufficient evidence for any particular one. An overview of the research and its implications for other members of the pectate lyase superfamily are presented.
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Herron, S.R., Jurnak, F. (2003). Mechanistic Lessons from Structural Studies of the Pectate Lyases. In: Voragen, F., Schols, H., Visser, R. (eds) Advances in Pectin and Pectinase Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0331-4_17
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DOI: https://doi.org/10.1007/978-94-017-0331-4_17
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