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The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937.
J Bacteriol. 1999 Jul; 181(13):3912-9.JB

Abstract

Erwinia chrysanthemi 3937 secretes into the external medium several pectinolytic enzymes, among which are eight isoenzymes of the endo-cleaving pectate lyases: PelA, PelB, PelC, PelD, and PelE (family 1); PelI (family 4); PelL (family 3); and PelZ (family 5). In addition, one exo-cleaving pectate lyase, PelX (family 3), has been found in the periplasm of E. chrysanthemi. The E. chrysanthemi 3937 gene kdgC has been shown to exhibit a high degree of similarity to the genes pelY of Yersinia pseudotuberculosis and pelB of Erwinia carotovora, which encode family 2 pectate lyases. However, no pectinolytic activity has been assigned to the KdgC protein. After verification of the corresponding nucleotide sequence, we cloned a longer DNA fragment and showed that this gene encodes a 553-amino-acid protein exhibiting an exo-cleaving pectate lyase activity. Thus, the kdgC gene was renamed pelW. PelW catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates. PelW is located in the bacterial cytoplasm. In this compartment, PelW action could complete the degradation of pectic oligomers that was initiated by the extracellular or periplasmic pectinases and precede the action of the cytoplasmic oligogalacturonate lyase, Ogl. Both cytoplasmic pectinases, PelW and Ogl, seem to act in sequence during oligogalacturonate depolymerization, since oligomers longer than dimers are very poor substrates for Ogl but are good substrates for PelW. The estimated number of binding subsites for PelW is three, extending from subsite -2 to +1, while it is probably two for Ogl, extending from subsite -1 to +1. The activities of the two cytoplasmic lyases, PelW and Ogl, are dependent on the presence of divalent cations, since both enzymes are inhibited by EDTA. In contrast to the extracellular pectate lyases, Ca2+ is unable to restore the activity of PelW or Ogl, while several other cations, including Co2+, Mn2+, and Ni2+, can activate both cytoplasmic lyases.

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Authors+Show Affiliations

Shevchik VE
Laboratoire de Génétique Moléculaire des Microorganismes et des Interactions Cellulaires, UMR-CNRS 5577, INSA, F-69621 Villeurbanne Cedex, France. shevchik@insa.insa-lyon.fr
Condemine G
No affiliation info available
Robert-Baudouy J
No affiliation info available
Hugouvieux-Cotte-Pattat N
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsCations, DivalentCell CompartmentationCytoplasmDickeya chrysanthemiEscherichia coliGenes, BacterialMolecular Sequence DataPectinsPolysaccharide-LyasesRecombinant ProteinsSequence Analysis, DNASequence Homology, Amino AcidSubstrate Specificity

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10383957

Citation

Shevchik, V E., et al. "The Exopolygalacturonate Lyase PelW and the Oligogalacturonate Lyase Ogl, Two Cytoplasmic Enzymes of Pectin Catabolism in Erwinia Chrysanthemi 3937." Journal of Bacteriology, vol. 181, no. 13, 1999, pp. 3912-9.
Shevchik VE, Condemine G, Robert-Baudouy J, et al. The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol. 1999;181(13):3912-9.
Shevchik, V. E., Condemine, G., Robert-Baudouy, J., & Hugouvieux-Cotte-Pattat, N. (1999). The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. Journal of Bacteriology, 181(13), 3912-9.
Shevchik VE, et al. The Exopolygalacturonate Lyase PelW and the Oligogalacturonate Lyase Ogl, Two Cytoplasmic Enzymes of Pectin Catabolism in Erwinia Chrysanthemi 3937. J Bacteriol. 1999;181(13):3912-9. PubMed PMID: 10383957.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. AU - Shevchik,V E, AU - Condemine,G, AU - Robert-Baudouy,J, AU - Hugouvieux-Cotte-Pattat,N, PY - 1999/6/29/pubmed PY - 1999/6/29/medline PY - 1999/6/29/entrez SP - 3912 EP - 9 JF - Journal of bacteriology JO - J Bacteriol VL - 181 IS - 13 N2 - Erwinia chrysanthemi 3937 secretes into the external medium several pectinolytic enzymes, among which are eight isoenzymes of the endo-cleaving pectate lyases: PelA, PelB, PelC, PelD, and PelE (family 1); PelI (family 4); PelL (family 3); and PelZ (family 5). In addition, one exo-cleaving pectate lyase, PelX (family 3), has been found in the periplasm of E. chrysanthemi. The E. chrysanthemi 3937 gene kdgC has been shown to exhibit a high degree of similarity to the genes pelY of Yersinia pseudotuberculosis and pelB of Erwinia carotovora, which encode family 2 pectate lyases. However, no pectinolytic activity has been assigned to the KdgC protein. After verification of the corresponding nucleotide sequence, we cloned a longer DNA fragment and showed that this gene encodes a 553-amino-acid protein exhibiting an exo-cleaving pectate lyase activity. Thus, the kdgC gene was renamed pelW. PelW catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates. PelW is located in the bacterial cytoplasm. In this compartment, PelW action could complete the degradation of pectic oligomers that was initiated by the extracellular or periplasmic pectinases and precede the action of the cytoplasmic oligogalacturonate lyase, Ogl. Both cytoplasmic pectinases, PelW and Ogl, seem to act in sequence during oligogalacturonate depolymerization, since oligomers longer than dimers are very poor substrates for Ogl but are good substrates for PelW. The estimated number of binding subsites for PelW is three, extending from subsite -2 to +1, while it is probably two for Ogl, extending from subsite -1 to +1. The activities of the two cytoplasmic lyases, PelW and Ogl, are dependent on the presence of divalent cations, since both enzymes are inhibited by EDTA. In contrast to the extracellular pectate lyases, Ca2+ is unable to restore the activity of PelW or Ogl, while several other cations, including Co2+, Mn2+, and Ni2+, can activate both cytoplasmic lyases. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/10383957/The_exopolygalacturonate_lyase_PelW_and_the_oligogalacturonate_lyase_Ogl_two_cytoplasmic_enzymes_of_pectin_catabolism_in_Erwinia_chrysanthemi_3937_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=10383957 DB - PRIME DP - Unbound Medicine ER -