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Chemical Compound Review

AC1L96YB     (2S,3R,4R,5R)-6- [(2S,3R,4R,5R,6S)-2...

Synonyms: 9046-40-6, |A-D-Polygalacturonic acid, Poly(1,4-|A-D-galacturonate)
 
 
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Disease relevance of alpha-D-polygalacturonic acid

 

High impact information on alpha-D-polygalacturonic acid

  • New domain motif: the structure of pectate lyase C, a secreted plant virulence factor [6].
  • Pectate lyases are secreted by pathogens and initiate soft-rot diseases in plants by cleaving polygalacturonate, a major component of the plant cell wall [6].
  • The bacterial regulator responsible for induction by plant extracts was identified and purified by using a DNA-binding assay with the promoter region of pelE that encodes a major pectate lyase [7].
  • The out genes of the enterobacterial plant pathogen Erwinia chrysanthemi are responsible for the efficient extracellular secretion of multiple plant cell wall-degrading enzymes, including four isozymes of pectate lyase, exo-poly-alpha-D-galacturonosidase, pectin methylesterase, and cellulase [8].
  • Pectate lyase treatment of sections resulted in an increased binding of cellulose-directed CBMs, demonstrating that decloaking cellulose microfibrils of pectic polymers can increase CBM access [9].
 

Chemical compound and disease context of alpha-D-polygalacturonic acid

  • One pectate lyase from Erwinia chrysanthemi (EC16), termed pectate lyase C, has been crystallized from ammonium sulfate [10].
  • Pectic enzymes in the supernatants of Erwinia chrysanthemi cultures in late-logarithmic-phase growth on D-galacturonan were resolved into three components: two pectate lyase isozymes and an exo-poly-alpha-D-galacturonosidase previously unreported in this organism [11].
  • Low iron availability is a triggering signal for coordinated expression of the genes encoding pectate lyases PelB, PelC, PelD, and PelE, and chrysobactin iron transport functions, which are two main determinants of phytopathogenicity of the Erwinia chrysanthemi strain 3937 [12].
  • Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine-rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes [13].
  • The pelB gene, which encodes one of the five pectate lyase isoenzymes of Erwinia chrysanthemi 3937, was mutagenized with a mini-Mu transposable element that can form gene fusions to the neomycin phosphotransferase-encoding region [14].
 

Biological context of alpha-D-polygalacturonic acid

  • Using high throughput screening of complex environmental DNA libraries more than 40 novel microbial pectate lyases were discovered, and their enzymatic properties were characterized [15].
  • Mild acid hydrolysis of a small (Mr = 6 kDa) pectic polysaccharide isolated from tomato leaves, an inducer of the synthesis and accumulation of two proteinase inhibitors in excised tomato plants, yielded a alpha-D-polygalacturonic acid polymer with degree of polymerization = 20 that retained proteinase inhibitor-inducing activity [16].
  • Insertion mutagenesis of the cloned region and recombination of the corresponding mutations in the bacterial chromosome by marker exchange revealed the existence of two divergently transcribed genes, pecS and pecM, that are both involved in the pectate lyase and cellulase regulation [17].
  • We have cloned a region involved in pectate lyase and cellulase secretion by complementation of non-secretory outJ mutants of E. chrysanthemi strain 3937 using the RP4::miniMu plasmid pULB110 [18].
  • When the TnphoA insertions were transferred back into E. chrysanthemi chromosome, the recombined strains no longer secreted pectate lyases or cellulases [18].
 

Anatomical context of alpha-D-polygalacturonic acid

  • Pectate lyases and the cellulase EGZ are rapidly degraded in the periplasm of the dsbA mutant [19].
  • It encodes a putative cytoplasmic membrane protein of 18.5 kDa that exhibits similarity to proteins required for extracellular secretion of pullulanase, pectate lyase or elastase in other Gram-bacteria [20].
  • We determined a 16-mer epitope peptide for the T-cell clone, and prepared synthetic oligopeptides of homologous regions in putative pectate lyase of other plants [21].
  • Conversion of liposomal 4-androsten-3,17-dione by A. simplex immobilized cells in calcium pectate [22].
  • Purification of pectate oligosaccharides showing root-growth-promoting activity in lettuce using ultrafiltration and nanofiltration membranes [23].
 

Associations of alpha-D-polygalacturonic acid with other chemical compounds

  • The functions of two of these genes are known: kduD codes for the 2-keto-3-deoxygluconate oxydoreductase and kdul for the 5-keto-4-deoxyuronate isomerase, two enzymes of the pectin degradation pathway. kdgC has 36% homology with pectate lyase genes of the periplasmic family but its product does not seem to have pectinolytic activity [24].
  • Chemical-modification and substrate-protection studies showed the presence of lysine and tryptophan at or near the active site of the pectate lyase [25].
  • Role of lysine, tryptophan and calcium in the beta-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae [25].
  • Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization [26].
  • Purification of pectate lyase produced by Colletotrichum gloeosporioides and its inhibition by epicatechin: a possible factor involved in the resistance of unripe avocado fruits to anthracnose [27].
 

Gene context of alpha-D-polygalacturonic acid

  • Moreover, pectate lyases expressed in an E. coli dsbA mutant were very instable but their stability was unaffected in a dsbC mutant [19].
  • This approach allowed us to isolate lacZ fusions with the genes pelC, pelD, ogl and pem, encoding pectate lyases PLc and PLd, oligogalacturonate lyase and pectin methylesterase, respectively [28].
  • Three classes of regulatory mutations responsible for constitutive pectate lyase synthesis have been described (kdgR, gpiR, and cri) [29].
  • Furthermore, we identified by DNA sequencing several other biocatalyst-encoding genes, including genes encoding a putative stereoselective amidase (amiA), two cellulases (gnuB and uvs080), an alpha-amylase (amyA), a 1,4-alpha-glucan branching enzyme (amyB), and two pectate lyases (pelA and uvs119) [30].
  • The enterobacterium Erwinia carotovora ssp. carotovora strain 71 (hereafter Ecc71) produces extracellular enzymes such as pectate lyase isozymes (Pels), cellulase (Cel), polygalacturonase (Peh) and protease (Prt) [31].
 

Analytical, diagnostic and therapeutic context of alpha-D-polygalacturonic acid

References

  1. Inducer of pectic acid lyase in Erwinia carotovora. Tsuyumu, S. Nature (1977) [Pubmed]
  2. Regulation of the Aspergillus nidulans pectate lyase gene (pelA). Dean, R.A., Timberlake, W.E. Plant Cell (1989) [Pubmed]
  3. The structure of Bacillus subtilis pectate lyase in complex with calcium. Pickersgill, R., Jenkins, J., Harris, G., Nasser, W., Robert-Baudouy, J. Nat. Struct. Biol. (1994) [Pubmed]
  4. Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome. Tamaru, Y., Doi, R.H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  5. Protein motifs. 3. The parallel beta helix and other coiled folds. Yoder, M.D., Jurnak, F. FASEB J. (1995) [Pubmed]
  6. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Yoder, M.D., Keen, N.T., Jurnak, F. Science (1993) [Pubmed]
  7. The pir gene of Erwinia chrysanthemi EC16 regulates hyperinduction of pectate lyase virulence genes in response to plant signals. Nomura, K., Nasser, W., Kawagishi, H., Tsuyumu, S. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  8. Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu. He, S.Y., Lindeberg, M., Chatterjee, A.K., Collmer, A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  9. Understanding the Biological Rationale for the Diversity of Cellulose-directed Carbohydrate-binding Modules in Prokaryotic Enzymes. Blake, A.W., McCartney, L., Flint, J.E., Bolam, D.N., Boraston, A.B., Gilbert, H.J., Knox, J.P. J. Biol. Chem. (2006) [Pubmed]
  10. Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi. Yoder, M.D., DeChaine, D.A., Jurnak, F. J. Biol. Chem. (1990) [Pubmed]
  11. An exo-poly-alpha-D-galacturonosidase implicated in the regulation of extracellular pectate lyase production in Erwinia chrysanthemi. Collmer, A., Whalen, C.H., Beer, S.V., Bateman, D.F. J. Bacteriol. (1982) [Pubmed]
  12. Iron regulation and pathogenicity in Erwinia chrysanthemi 3937: role of the Fur repressor protein. Franza, T., Sauvage, C., Expert, D. Mol. Plant Microbe Interact. (1999) [Pubmed]
  13. Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine-rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes. Alfano, J.R., Ham, J.H., Collmer, A. J. Bacteriol. (1995) [Pubmed]
  14. Pectate lyase gene regulatory mutants of Erwinia chrysanthemi. Diolez, A., Richaud, F., Coleno, A. J. Bacteriol. (1986) [Pubmed]
  15. Discovery of pectin-degrading enzymes and directed evolution of a novel pectate lyase for processing cotton fabric. Solbak, A.I., Richardson, T.H., McCann, R.T., Kline, K.A., Bartnek, F., Tomlinson, G., Tan, X., Parra-Gessert, L., Frey, G.J., Podar, M., Luginbühl, P., Gray, K.A., Mathur, E.J., Robertson, D.E., Burk, M.J., Hazlewood, G.P., Short, J.M., Kerovuo, J. J. Biol. Chem. (2005) [Pubmed]
  16. Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments. Bishop, P.D., Pearce, G., Bryant, J.E., Ryan, C.A. J. Biol. Chem. (1984) [Pubmed]
  17. pecS: a locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi. Reverchon, S., Nasser, W., Robert-Baudouy, J. Mol. Microbiol. (1994) [Pubmed]
  18. Molecular cloning of the outJ gene involved in pectate lyase secretion by Erwinia chrysanthemi. Ji, J., Hugouvieux-Cotte-Pattat, N., Robert-Baudouy, J. Mol. Microbiol. (1989) [Pubmed]
  19. Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi. Shevchik, V.E., Bortoli-German, I., Robert-Baudouy, J., Robinet, S., Barras, F., Condemine, G. Mol. Microbiol. (1995) [Pubmed]
  20. Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae. Overbye, L.J., Sandkvist, M., Bagdasarian, M. Gene (1993) [Pubmed]
  21. Survival of memory T cells specific for Japanese cypress pollen allergen is maintained by cross-stimulation of putative pectate lyases from other plants. Nakamura, Y., Takagi, S., Suzuki, M., Ito, H., Murakami, S., Ohta, N. Allergy (2001) [Pubmed]
  22. Conversion of liposomal 4-androsten-3,17-dione by A. simplex immobilized cells in calcium pectate. Llanes, N., Pendás, J., Falero, A., Pérez, C., Hung, B.R., Moreira, T. J. Steroid Biochem. Mol. Biol. (2002) [Pubmed]
  23. Purification of pectate oligosaccharides showing root-growth-promoting activity in lettuce using ultrafiltration and nanofiltration membranes. Iwasaki, K.I., Matsubara, Y. J. Biosci. Bioeng. (2000) [Pubmed]
  24. Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation. Condemine, G., Robert-Baudouy, J. Mol. Microbiol. (1991) [Pubmed]
  25. Role of lysine, tryptophan and calcium in the beta-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae. Rao, M.N., Kembhavi, A.A., Pant, A. Biochem. J. (1996) [Pubmed]
  26. Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization. Kamen, D.E., Woody, R.W. Biochemistry (2002) [Pubmed]
  27. Purification of pectate lyase produced by Colletotrichum gloeosporioides and its inhibition by epicatechin: a possible factor involved in the resistance of unripe avocado fruits to anthracnose. Wattad, C., Dinoor, A., Prusky, D. Mol. Plant Microbe Interact. (1994) [Pubmed]
  28. Isolation of Erwinia chrysanthemi mutants altered in pectinolytic enzyme production. Hugouvieux-Cotte-Pattat, N., Robert-Baudouy, J. Mol. Microbiol. (1989) [Pubmed]
  29. Regulation of expression of pectate lyase genes pelA, pelD, and pelE in Erwinia chrysanthemi. Reverchon, S., Robert-Baudouy, J. J. Bacteriol. (1987) [Pubmed]
  30. Prospecting for novel biocatalysts in a soil metagenome. Voget, S., Leggewie, C., Uesbeck, A., Raasch, C., Jaeger, K.E., Streit, W.R. Appl. Environ. Microbiol. (2003) [Pubmed]
  31. Characterization of a novel RNA regulator of Erwinia carotovora ssp. carotovora that controls production of extracellular enzymes and secondary metabolites. Liu, Y., Cui, Y., Mukherjee, A., Chatterjee, A.K. Mol. Microbiol. (1998) [Pubmed]
  32. Is Congo red an amyloid-specific dye? Khurana, R., Uversky, V.N., Nielsen, L., Fink, A.L. J. Biol. Chem. (2001) [Pubmed]
  33. Crystallization and preliminary X-ray studies of the pectate lyase from Bacillus subtilis. Jenkins, J., Nasser, W., Scott, M., Pickersgill, R., Vignon, J.C., Robert-Baudouy, J. J. Mol. Biol. (1992) [Pubmed]
  34. Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Henrissat, B., Heffron, S.E., Yoder, M.D., Lietzke, S.E., Jurnak, F. Plant Physiol. (1995) [Pubmed]
  35. Identification of a polygalacturonase as a major allergen (Pla a 2) from Platanus acerifolia pollen. Ibarrola, I., Arilla, M.C., Martínez, A., Asturias, J.A. J. Allergy Clin. Immunol. (2004) [Pubmed]
 
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