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. 1992 Mar;174(6):2039–2042. doi: 10.1128/jb.174.6.2039-2042.1992

Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemi EC16.

J F Preston 3rd 1, J D Rice 1, L O Ingram 1, N T Keen 1
PMCID: PMC205812  PMID: 1548242

Abstract

The four pectate lyases (EC 4.2.2.2) secreted by Erwinia chrysanthemi EC16 have been individually produced as recombinant enzymes in Escherichia coli. Oligogalacturonates formed from polygalacturonic acid during reactions catalyzed by each enzyme have been determined by high-performance liquid chromatography analysis. PLa catalyzes the formation of a series of oligomers ranging from dimer to dodecamer through a random endolytic depolarization mechanism. PLb and PLc are trimer- and tetramer-generating enzymes with an identical combination of endolytic and exolytic mechanisms. PLe catalyzes a nonrandom endolytic depolymerization with the formation of dimer as the predominant product. The pectate lyases secreted by E. chrysanthemi EC16 represent a battery of enzymes with three distinct approaches to the depolymerization of plant cell walls.

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Selected References

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