Literature summary for 3.2.1.55 extracted from

Shallom, D.; Belakhov, V.; Solomon, D.; Shoham, G.; Baasov, T.; Shoham, Y.
Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase (2002), J. Biol. Chem., 277, 43667-43673.

Search for more literature for 3.2.1.55

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)	Geobacillus stearothermophilus

Protein Variants

Protein Variants	Comment	Organism
E175A	site-directed mutagenesis, altered kinetic properties	Geobacillus stearothermophilus
E294A	site-directed mutagenesis, reduced activity and about 10fold increased Km for substrate 2',4',6'-trichlorophenyl alpha-L-arabinofuranoside compared to the wild-type enzyme	Geobacillus stearothermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
3',4'-dinitrophenyl alpha-L-arabinofuranoside	uncompetitive substrate inhibition occurs at high concentrations	Geobacillus stearothermophilus
3-nitrophenyl-alpha-L-arabinofuranoside	uncompetitive substrate inhibition occurs at high concentrations	Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	detailed kinetic study, overview	Geobacillus stearothermophilus
0.003	-	2',5'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.01	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.01	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
0.04	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.14	-	4-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.35	-	2',5'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
0.53	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
0.6	-	3-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.65	-	4-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
1.7	-	3-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Sodium azide	activates the wild-type enzyme over 40fold	Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Geobacillus stearothermophilus	key enzyme in the complete degradation of the plant cell wall, enzyme is a hemicellulose, probable mechanistic pathway	?	-	?
additional information	Geobacillus stearothermophilus T-6	key enzyme in the complete degradation of the plant cell wall, enzyme is a hemicellulose, probable mechanistic pathway	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	Q9XBQ3	gene abfA	-
Geobacillus stearothermophilus T-6	Q9XBQ3	gene abfA	-

Reaction

Reaction	Comment	Organism	Reaction ID
1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	catalytic mechanism, Glu175 is the acid-base residue, Glu294 functions as the catalytic nucleophile	Geobacillus stearothermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	2,4,6-trichlorophenol + alpha-L-arabinofuranose	-	r
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus T-6	2,4,6-trichlorophenol + alpha-L-arabinofuranose	-	r
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	2',4',6'-trichlorophenol + alpha-L-arabinofuranose	-	?
2',5'-dinitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	2,5-dinitrophenol + alpha-L-arabinofuranose	-	r
2',5'-dinitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus T-6	2,5-dinitrophenol + alpha-L-arabinofuranose	-	r
2,5-dinitrophenyl-alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	2,5-dinitrophenol + L-arabinofuranose	-	?
3',4''-dinitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	3',4''-dinitrophenol + alpha-L-arabinofuranose	-	?
3',4'-dinitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	3',4'-dinitrophenol + alpha-L-arabinofuranose	-	r
3-nitrophenyl-alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	3-nitrophenol + alpha-L-arabinofuranose	-	r
4-nitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	4-nitrophenol + alpha-L-arabinofuranose	-	r
4-nitrophenyl alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus T-6	4-nitrophenol + alpha-L-arabinofuranose	-	r
m-nitrophenyl-alpha-L-arabinofuranoside + H2O	-	Geobacillus stearothermophilus	m-nitrophenol + L-arabinofuranose	-	?
additional information	key enzyme in the complete degradation of the plant cell wall, enzyme is a hemicellulose, probable mechanistic pathway	Geobacillus stearothermophilus	?	-	?
additional information	stereochemistry of the reversible hydrolytic reaction, enzyme performs glycosyl transfer to low molecular weight alcohols	Geobacillus stearothermophilus	?	-	?
additional information	key enzyme in the complete degradation of the plant cell wall, enzyme is a hemicellulose, probable mechanistic pathway	Geobacillus stearothermophilus T-6	?	-	?
additional information	stereochemistry of the reversible hydrolytic reaction, enzyme performs glycosyl transfer to low molecular weight alcohols	Geobacillus stearothermophilus T-6	?	-	?

Synonyms

Synonyms	Comment	Organism
alpha-L-arabinofuranosidase	-	Geobacillus stearothermophilus
More	enzyme belongs to the family 51 of glycoside hydrolases	Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	assay at	Geobacillus stearothermophilus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
40	70	-	Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kcat with mutant 294A	Geobacillus stearothermophilus
0.0041	-	3-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.08	-	4-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.24	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.66	-	3',4'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
0.72	-	2',5'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, mutant E175A	Geobacillus stearothermophilus
65	-	2',4',6'-trichlorophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
83	-	3-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
87	-	4-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
190	-	2',5'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
340	-	3',4'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	assay at	Geobacillus stearothermophilus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
10	-	3-nitrophenyl-alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus
12	-	3',4'-dinitrophenyl alpha-L-arabinofuranoside	pH 6.0, 40°C, wild-type enzyme	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)