3.2.1.164: galactan endo-1,6-beta-galactosidase
This is an abbreviated version!
For detailed information about galactan endo-1,6-beta-galactosidase, go to the full flat file.
Word Map on EC 3.2.1.164
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3.2.1.164
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galactose
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oligosaccharides
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helicase
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larch
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wood
- 3.2.1.164
- galactose
- oligosaccharides
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helicase
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larch
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wood
Reaction
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products =
Synonyms
6GAL, beta-(1,6)-galactanase, beta-1,6-galactanase, beta-D-galactanase, ebg, endo-beta-(1,6)-D-galactanase, endo-beta-(1-6)-D-galactanase, endo-beta-(1-6)-galactanase, endo-beta-(1->6)-D-galactanase, endo-beta-(1->6)-galactanase, endo-beta-1,6-D-galactanase, endo-beta-1,6-galactanase, GAL1, More, Tv6GAL, type II arabinogalactan-degrading enzyme
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General Information
General Information on EC 3.2.1.164 - galactan endo-1,6-beta-galactosidase
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evolution
the enzyme belongs to the glycosylhydrolase family 30, GH30
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
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