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Literature summary for 3.2.1.164 extracted from

  • Villa-Rivera, M.; Zavala-Paramo, M.; Conejo-Saucedo, U.; Lopez-Romero, E.; Lara-Marquez, A.; Cano-Camacho, H.
    Differences in the expression profile of endo-beta-(1,6)-D-galactanase in pathogenic and non-pathogenic races of Colletotrichum lindemuthianum grown in the presence of arabinogalactan, xylan or Phaseolus vulgaris cell walls (2017), Physiol.Mol. Plant Pathol., 99, 75-86 .
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Cloned(Commentary)

Cloned (Comment) Organism
gene ebg, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of enzyme EBG from races 0 and 1472 in Escherichia coli TOP10 Colletotrichum lindemuthianum

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
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 Colletotrichum lindemuthianum 5618
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extracellular the enzyme contains an N-terminal secretion signal Colletotrichum lindemuthianum
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arabinogalactan + H2O Colletotrichum lindemuthianum
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 oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
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 ?

Organism

Organism UniProt Comment Textmining
Colletotrichum lindemuthianum A0A1L2S4I5 i.e. Glomerella lindemuthiana, pathogenic race 1472 and non-pathogenic race 0
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme contains 3 putative N-glycosylation sites at Asp45, Asp233, and Asp416 Colletotrichum lindemuthianum

Source Tissue

Source Tissue Comment Organism Textmining
additional information growth of both races with glucose show basal transcription levels of enzyme. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increases in pathogenic race 1472 but not in non-pathogenic race 0 Colletotrichum lindemuthianum
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mycelium
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 Colletotrichum lindemuthianum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arabinogalactan + H2O
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 Colletotrichum lindemuthianum oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
-
 ?
arabinogalactan + H2O plant type II arabinogalactans consisting of beta-(1,3)- and beta-(1,6)-galactan side chains connected to each other by (1,3)(1,6)-linked branch points. The O-3 and O-6 positions are substituted with terminal arabinosyl residues Colletotrichum lindemuthianum oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
-
 ?

Synonyms

Synonyms Comment Organism
ebg
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 Colletotrichum lindemuthianum
endo-beta-(1,6)-D-galactanase
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 Colletotrichum lindemuthianum
endo-beta-1,6-galactanase
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 Colletotrichum lindemuthianum

Expression

Organism Comment Expression
Colletotrichum lindemuthianum growth of both races with glucose show basal transcription levels of ebg. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increased in pathogenic race 1472 but not in non-pathogenic race 0 additional information

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycosylhydrolase family 30, GH30 Colletotrichum lindemuthianum
additional information putative DNA-binding sites for Cre, Xlnr, ACEI, PacC and Gal4 transcriptional factors are predicted in ebg genes from Colletotrichum species. Identification of potential functional and structural domains, protein structure homology modelling and structure comaprisons. In enzyme EBG, the catalytic proton donor E191 is positioned in a coil and the catalytic nucleophile E293 is positioned in a beta-strand Colletotrichum lindemuthianum
physiological function endo-breta-(1,6)-D-galactanase is a debranching hemicellulase that catalyzes the hydrolysis of beta-(1,6)-galactosyl side chains in arabinogalactans (AGs), producing beta-(1,6)-galacto-oligomers and beta-(1,6)-D-galactobiose. The enzyme plays a critical role in cell wall degradation. Arabinogalactan proteins (AGPs) are putative co-receptors in signaling pathways that function during growth and plant developmen. AGPs also play a key role in both beneficial and pathogenic root-microorganism interactions. They are essential for root cells to recognize beneficial microorganisms as well for root cells to trigger localized and efficient defense responses to control pathogenic organisms. Since the carbohydrate groups in AGPs are critical for their function, it is conceivable to hypothesize that the pathogenic race of Colletotrichum lindemuthianum, which more rapidly expresses gene ebg at higher levels in the presence of plant cell wall polysaccharides, is better adapted to degrade AGPs for the establishment of the infection as the non-pathogenic race Colletotrichum lindemuthianum