Literature summary for 3.2.1.37 extracted from

Shallom, D.; Leon, M.; Bravman, T.; Ben-David, A.; Zaide, G.; Belakhov, V.; Shoham, G.; Schomburg, D.; Baasov, T.; Shoham, Y.
Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6 (2005), Biochemistry, 44, 387-397.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene xynB3, expression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Geobacillus stearothermophilus

Protein Variants

Protein Variants	Comment	Organism
D128G	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, nearly inactive mutant	Geobacillus stearothermophilus
D15G	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, nearly inactive mutant	Geobacillus stearothermophilus
E178G	site-directed mutagenesis, the mutant shows an altered substrate specificity and highly reduced activity compared to the wild-type enzyme	Geobacillus stearothermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
Ag+	97% inhibition at 1 mM	Geobacillus stearothermophilus
Hg2+	complete inhibition at 1 mM, 93% inhibition at 0.1 mM	Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics, recombinant wild-type and mutant enzymes	Geobacillus stearothermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	the enzyme is not affected by 1 mM of Fe3+, Ca2+, Co2+, Mg2+, Ba2+, Ni2+, K+, Zn2+, Cu2+, or EDTA	Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
180000	-	gel filtration	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	Q09LX0	i.e. Bacillus stearothermophilus, strain T-6, gene xynB3	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant soluble wild-type, 2.6fold to over 95% purity, and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment and gel filtration	Geobacillus stearothermophilus

Reaction

Reaction	Comment	Organism	Reaction ID
(Xylbeta(1-4))x + H2O = beta-D-xylopyranose + (Xylbeta(1-4))x-1	catalytic residues D15, D128, and E187 are essential for activity, reaction mechanism	Geobacillus stearothermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O	-	Geobacillus stearothermophilus	2,5-dinitrophenol + beta-D-xylose	-	?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O	-	Geobacillus stearothermophilus	3,4-dinitrophenol + beta-D-xylopyranose	-	?
3,5-dinitrophenyl beta-D-xylopyranoside + H2O	-	Geobacillus stearothermophilus	3,5-dinitrophenol + beta-D-xylose	-	?
4-bromophenyl-beta-D-xylopyranoside + H2O	low activity of mutant E178G, no activity of the wild-type enzyme	Geobacillus stearothermophilus	4-bromophenol + beta-D-xylose	-	?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O	-	Geobacillus stearothermophilus	4-methylumbelliferol + beta-D-xylose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	-	Geobacillus stearothermophilus	4-nitrophenol + beta-D-xylose	-	?
additional information	substrate specificity of wild-type enzyme and mutant E178G, the mutant enzyme shows residual activity with 2-naphthyl-beta-D-xylopyranoside, 3,4-dimethylphenyl-beta-D-xylopyranoside, and 3-nitrophenyl-beta-D-xylopyranoside, while the wild-type enzyme is inactive with these substrates, overview	Geobacillus stearothermophilus	?	-	?

Subunits

Subunits	Comment	Organism
trimer	in solution	Geobacillus stearothermophilus

Synonyms

Synonyms	Comment	Organism
beta-D-xylosidase	-	Geobacillus stearothermophilus
More	the enzyme belongs to the glycosyl hydrolase family 43, GH43	Geobacillus stearothermophilus
XynB3	-	Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	-	Geobacillus stearothermophilus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
additional information	-	temperature profile and thermal stability	Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	temperature profile and thermal stability	Geobacillus stearothermophilus
60	-	fully stable up to	Geobacillus stearothermophilus
75	-	inactivation	Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.014	-	4-nitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant mutant E178G	Geobacillus stearothermophilus
1.8	-	3,4-dinitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant mutant E178G	Geobacillus stearothermophilus
20	-	4-methylumbelliferyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant wild-type enzyme	Geobacillus stearothermophilus
25	-	2,5-dinitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant wild-type enzyme	Geobacillus stearothermophilus
30	-	2,5-dinitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant mutant E178G	Geobacillus stearothermophilus
57	-	4-nitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant wild-type enzyme	Geobacillus stearothermophilus
77	-	3,4-dinitrophenyl-beta-D-xylopyranoside	pH 7.0, 40°C, recombinant wild-type enzyme	Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	-	-	Geobacillus stearothermophilus

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	pH profiles, wild-type and mutant enzymes, overview	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)