Poly-D-Galacturonate Lyases

The poly-D-galacturonate lyase and pectinesterase activities of Clostridium multifermentans appear to be associated in a single complex. Kinetic data suggested that the enzymes act on their respective substrates by a single-chain 

Rexovd-Benkova, O. Lukndr, and L. Kuniak, Coll. Czech. Chem. Comm., 1976,41, 1879. M. J. Foglietti, H. Girerd, and F. Percheron, Biochimie, 1975, 57, 667. 

In a procedure described for the simultaneous large-scale isolation of pullulanase and (1 4)-oc-D-glucan phosphorylase from Klebsiella pneumoniae, the pullulanase is solubilized from the cell wall by cholate treatment cells and cell debris are removed by partition in a poly(ethyleneglycol)-dextran two-phase system and from the upper phase of this system the pullulanase is isolated by ultrafiltration and precipitation with A -cetyl-iV, A -trimethylammonium bromide to 80% purity with 70% yield and in an a-amylase-free state. 

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Various enterobacteria have been shown to exhibit several patterns of biosynthesis and excretion of poly-D-galacturonate lyase.In a strain of Erwinia chrysanthemi, poly-D-galacturonate lyase is an extracellular enzyme and is almost totally excreted. In strains of Yersinia enterocolitica and Yersinia pseudotuberculosis poly-D-galacturonate lyase is a periplasmic and cytoplasmic enzyme. 

The poly-D-galacturonate lyase associated with healthy and Gloeosporium papayae rot infected papaya Carieca papaya) fruit, and secreted in papaya pulp medium by the pathogen has been investigated. ... 

Together with poly-D-galacturonase and poly-D-galacturonate lyase, pectinesterase has been found in cultures of large spiral organisms (Treponemes) from the serum of cattle. ... 

A poly-D-galacturonate lyase released from Erwinia rubrifaciens cells by osmotic shock has been purified by ion-exchange chromatography and isoelectric focusing. The purified enzyme (mol. wt. 4.1 x 10", S optimum 9.5, temperature optimum 37 °C) requires Ca ions, for activity and prefers unmethylated poly(D-galacturonic acid) as a substrate. Ways of releasing more of the enzyme from the cells were reported. 

Pseudomonas cepacia growing in continuous culture at pH 7 synthesized a poly-D-galacturonate lyase. 

Deoxy- -L-//rreo-hex-4-enepyranosyluronic acid)-D-galacturonic acid has been proposed as the inducer of pectic acid (poly-D-galacturonate) lyase in Erwinia carotovora. No induction was observed for D-galacturonic acid. 

The action of a storage rot pathogen (Phoma betae) on harvested sugar beets (Beta vulgaris) depends, in part, on the synthesis of an eudo-poly-D-galacturonate lyase. ... 

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