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Literature summary for 3.2.1.8 extracted from

  • Geiser, E.; Wierckx, N.; Zimmermann, M.; Blank, L.
    Identification of an endo-1,4-beta-xylanase of Ustilago maydis (2013), BMC Biotechnol., 13, 59.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Ustilago maydis Q4P0L3
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-
Ustilago maydis 521 Q4P0L3
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xylan + H2O
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Ustilago maydis xylotriose + ? after 25 h of reaction only xylotriose is left in the supernatant. No xylobiose or xylose are detected ?
xylan + H2O
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Ustilago maydis 521 xylotriose + ? after 25 h of reaction only xylotriose is left in the supernatant. No xylobiose or xylose are detected ?

Synonyms

Synonyms Comment Organism
Xyn11A
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Ustilago maydis

General Information

General Information Comment Organism
physiological function deletion of the gene encoding xylanase 11A reduces the growth rate of the mutant on minimal medium with xylan to 0.09 per h compared to 0.10 per h of the wild-type. The deletion mutant reaches a final OD600 of 6.78 compared to 8.18 in the wild-type culture. The drop of the pH value from initially 5.7 to 3.4 is approximately 3 h delayed in comparison to wild-type. Also the maximal concentration of reducing sugars in the medium is lower, and occurs 9 h later than in the wildtype culture. Heterologous expression of xylanase 11A on the cell surface of a xylanase-negative strain of Saccharomyces cerevisiae enables the strain to almost completely degrade xylan to xylotriose Ustilago maydis