Literature summary for 3.2.1.8 extracted from

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 (2009), Biosci. Biotechnol. Biochem., 73, 965-967.

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Cloned(Commentary)

Cloned (Comment)	Organism
plasmids pET-DELTAXBD, pET-DELTAXBDR5 and pET-DELTAXBDK51R/R5 expressed in Escherichia coli BL21(DE3)	Bacillus sp. 41M-1

Protein Variants

Protein Variants	Comment	Organism
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	Bacillus sp. 41M-1

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. 41M-1	Q9RC94	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
birchwood xylan + H2O	-	Bacillus sp. 41M-1	?	-	?

Synonyms

Synonyms	Comment	Organism
xylanase J	-	Bacillus sp. 41M-1
XynJ	-	Bacillus sp. 41M-1

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
55	-	wild-type DELTAXBD	Bacillus sp. 41M-1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	wild-type DELTAXBD	Bacillus sp. 41M-1

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Release 2023.1 (January 2023)