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EC Tree
The taxonomic range for the selected organisms is: Bacillus sp. 41M-1 The enzyme appears in selected viruses and cellular organisms
Synonyms
endoxylanase, xylanase a, endo-xylanase, xyn11a, xyn10a, beta-xylanase, endo-1,4-beta-xylanase, gh11 xylanase, xylanase b, xynii,
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(1--> 4)-beta-xylan 4-xylanohydrolase
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1,4-beta-D-xylan xylanohydrolase
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1,4-beta-D-xylan xylanohydrolase 22
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1,4-beta-xylan xylanohydrolase
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beta-1,4-D-xylanase
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beta-1,4-xylan xylanohydrolase
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beta-1,4-xylanase
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endo-(1--> 4)-beta-xylanase
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endo-1,4-beta-D-xylanase
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endo-1,4-beta-xylanase
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endo-1,4-xylanase
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endo-beta-1,4-xylanase
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xylanase, endo-1,4-
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4-beta-D-xylan xylanohydrolase
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birchwood xylan + H2O
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Uniprot
brenda
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Q9RC94_9BACI
354
0
39000
TrEMBL
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additional information
DELTAXBD, consists of the catalytic domain only and corresponds to ALa1-Pro222 of XynJ. Mutants DELTAXBDR5 and DELTAXBDK51R/R5 show about 50% activity of that of DELTAXBD and have optima of pH 9.0 and 9.5, respectively. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shift the optimum pH of the wild-type enzyme from 8.5 to 9.5. Mutant DELTAXBDK51R exhibit almost the same temperature profile and temperature optimum as DELTAXBD. The temperature optima of mutants DELTAXBDR5 and DELTAXBDK51R/R5 are both 60°C. Mutants show lower specific activity than DELTAXBD at 37-60°C, but they show apparently higher activity at 65°C. Introduction of excess Arg residues on the protein surface increase the thermostability of DELTAXBD
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plasmids pET-DELTAXBD, pET-DELTAXBDR5 and pET-DELTAXBDK51R/R5 expressed in Escherichia coli BL21(DE3)
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Umemoto, H.; Ihsanawati, H.; Inami, M.; Yatsunami, R.; Fukui, T.; Kumasaka, T.; Tanaka, N.; Nakamura, S.
Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface
Biosci. Biotechnol. Biochem.
73
965-967
2009
Bacillus sp. 41M-1 (Q9RC94)
brenda