Exopectic Acid Transeliminase of an Erwinia

Hatanaka, Chitoshi; Ozawa, Junjiro

doi:10.1271/bbb1961.36.2307

Cited by 10 publications

(8 citation statements)

References 4 publications

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“…4 ) In the present study, a similar result was also obtained, although a commercial preparation of citrus pectin was used as the carbon source instead of pectic acid. This observation is favorable because the pectinmedium is more economical than the pectate one.…”

Section: Discussionsupporting

confidence: 81%

Affinity Chromatography of Exopolygalacturonate Lyase fromErwinia carotovorasubsp.carotovora

Kegoya

Setoguchi²,

Yokohiki³

et al. 1984

Agricultural and Biological Chemistry

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Section: Discussionsupporting

confidence: 81%

Affinity Chromatography of Exopolygalacturonate Lyase fromErwinia carotovorasubsp.carotovora

Kegoya

Setoguchi²,

Yokohiki³

et al. 1984

Agricultural and Biological Chemistry

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“…The presence of a signal peptide suggests that the enzyme is exported at least to the periplasm in E. chrysanthemi. A periplasmic ExoPL would be expected to cleave oligogalacturonates in addition to polygalacturonate, as reported previously for the ExoPL produced by E. carotovora (17) and for the ExoPL produced by E. chrysanthemi CUCPB1237 (9). The enzyme would thus complement the activity of cytoplasmic oligogalacturonide lyase in the catabolism of oligogalacturonates.…”

mentioning

confidence: 60%

“…Link pectin was prepared in acidified methanol by the method of Morell (31,32). ExoPL activity was determined by monitoring the A232 of a reaction mixture containing 0.15% (wt/vol) Tris pectate (pectate titrated with Tris base to pH 7.5), 70 mM NaCl, 0.075 mM CaCl2, and 0.1 mM MnCl2 (17).…”

mentioning

confidence: 99%

Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product

Brooks

Gold

et al. 1990

J Bacteriol

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The ability of Erwinia chrysanthemi to cause soft-rot diseases involving tissue maceration in many plants has been linked to the production of endo-pectate lyase E. chrysanthemi EC16 mutant UM1005, however, contains deletions in the pel genes that encode the known endopectate lyases, yet still macerates plant tissues. In an attempt to identify the remaining macerating factor(s), a gene library of UM1005 was constructed in Escherichia coli and screened for pectolytic activity. A clone (pPNL5) was identified in this library that contained the structural gene for an exopolygalacturonate lyase (ExoPL). The gene for ExoPL was localized on a 3.3-kb EcoRV fragment which contained an open reading frame for a 79,500-Da polypeptide. ExoPL was purified to apparent homogeneity from Escherichia coli DH5 alpha (pPNL5) and found to have an apparent molecular weight of 76,000 with an isoelectric point of 8.6. Purified ExoPL had optimal activity between pH 7.5 and 8.0 and could utilize pectate, citrus pectin, and highly methyl-esterified Link pectin as substrates. A PL- ExoPL- mutant of EC16 was constructed that exhibited reduced growth on pectate, but retained pathogenicity on chrysanthemum equivalent to that of UM1005. The results indicate that ExoPL does not contribute to the residual macerating activity of UM1005.

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“…So far exopolygalacturonate lyase has been found only as an extra cellular enzyme from bacterial sources [Clostridium multifermentans (43,44,45,85,87), Erwinia aroideae (46,49), and an Erwinia species (165)]. Macmillan and Vaughn (43,44) partially purified the clostridial enzyme from culture broth and freed it of accompanying pectinesterase activity.…”

Section: Exopolygalacturonate Lyasementioning

confidence: 99%

Pectic Enzymes

Macmillan

SHEIMAN

1974

Advances in Chemistry

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Pectic substances, largely polygalacturonic acid or its methyl ester, are found in the primary cell walls of plants and in the middle lamella. Enzymes from plants, fungi, and bacteria degrade pectic substances and cause plant tissue maceration by esterase action on the methyl ester groups or by glycosidase or lyase action on the polygalacturonate chain. Numer ous enzymes are distinguished from one another by mecha nism (hydrolysis or trans elimination), specificity (pectin, polygalacturonate, oligogalacturonates, Δ4:5 unsaturated oligogalacturonates), action pattern (endo or exo), and stimu lation by cations. Pectic enzymes are used commercially in producing fruit juices and wines. Fundamental proper ties of the enzymes are discussed with reference to their applications in food processes. This review is primarily concerned with fundamental properties of the A pectic enzymes with some reference to their role in nature and to their applications in food processing. Because of the vast amount of literature in this field the reader is directed to other articles and books on the chemistry of pectic substances and the enzymes which degrade them Pectic substances are found in the tissues of higher plants where they have an important structural role. They are deposited in the primary cell wall during the early stages of growth and in the middle lamella where they act as "intercellular cement." The enzymatic breakdown of pectic substances in the middle lamella leads to plant tissue maceration. There fore the enzymes that degrade pectin are involved in natural processes such as the ripening of fruit (22, 23), abscission of leaves and plant organs (24), invasion of tissues by plant pathogens (6), and in the spoil age of fruits and vegetables ( 25, 26, 27 ). They are essential in the rapid decay of dead plant material and undoubtedly assist in recycling carbon (1-21).

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Exopectic Acid Transeliminase of an Erwinia

Abstract: A species of Eruwinia was found to produce no other pectolytic enzyme than the two transeliminases of exo-types, namely, an oligogalacturonide transeliminase and an exopectic acid transeliminase. Of the two enzymes, the exopectic acid transeliminase was isolated and

Cited by 10 publications

References 4 publications

Affinity Chromatography of Exopolygalacturonate Lyase fromErwinia carotovorasubsp.carotovora

Affinity Chromatography of Exopolygalacturonate Lyase fromErwinia carotovorasubsp.carotovora

Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product

Pectic Enzymes

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