Literature summary for 3.2.1.55 extracted from

Dumbrepatil, A.; Park, J.M.; Jung, T.Y.; Song, H.N.; Jang, M.U.; Han, N.S.; Kim, T.J.; Woo, E.J.
Structural analysis of alpha-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity (2012), J. Microbiol. Biotechnol., 22, 1724-1730.

Cloned(Commentary)

Cloned (Comment)	Organism
constitutive recombinant expression of His-tagged enzyme in Escherichia coli strain MC1061	Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged enzyme in complex with a branched tetrasaccharide O-beta-D-xylopyranosyl-(1->4)-O-alpha-L-arabinofuranosyl-(1->3)-O-beta-D-xylopyranosyl-(1->4)-O-beta-D-xylopyranoside, sitting drop vapor-diffusion method, mixing 0.0015 ml of protein solution containing 14 mg/ml protein, 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 5.0% 2-mercaptoethanol, with an equal volume of the reservoir solution, 16.1°C, X-ray diffraction structure determination and analysis	Thermotoga maritima

Crystallization (Comment)

Organism

purified recombinant His-tagged enzyme in complex with a branched tetrasaccharide O-beta-D-xylopyranosyl-(1->4)-O-alpha-L-arabinofuranosyl-(1->3)-O-beta-D-xylopyranosyl-(1->4)-O-beta-D-xylopyranoside, sitting drop vapor-diffusion method, mixing 0.0015 ml of protein solution containing 14 mg/ml protein, 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 5.0% 2-mercaptoethanol, with an equal volume of the reservoir solution, 16.1°C, X-ray diffraction structure determination and analysis

Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
L-arabinan + H2O	Thermotoga maritima	-	?	-	?
L-arabinan + H2O	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	-	?	-	?
L-arabinoxylan + H2O	Thermotoga maritima	-	?	-	?
L-arabinoxylan + H2O	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	-	?	-	?
additional information	Thermotoga maritima	a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes	?	-	?
additional information	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9WYB7	-	-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	Q9WYB7	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography, dialysis, and gel filtration, to homogeneity	Thermotoga maritima

Reaction

Reaction	Comment	Organism	Reaction ID
1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	the enzyme hydrolyze the glycosidic bond via the double-displacement mechanism in the active site of a funnel-shaped pocket, catalytic residues are the acid/base Glu172 and the enzymatic nucleophile Glu281	Thermotoga maritima	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
L-arabinan + H2O	-	Thermotoga maritima	?	-	?
L-arabinan + H2O	-	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	?	-	?
L-arabinoxylan + H2O	-	Thermotoga maritima	?	-	?
L-arabinoxylan + H2O	-	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	?	-	?
additional information	a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes	Thermotoga maritima	?	-	?
additional information	a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview	Thermotoga maritima

Synonyms

Synonyms	Comment	Organism
alpha-L-arabinofuranosidase	-	Thermotoga maritima
TmAFase	-	Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
80	-	-	Thermotoga maritima

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	-	Thermotoga maritima

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the glycoside hydrolase 51 family, GH51	Thermotoga maritima
additional information	tight domain associations found in the enzyme, such as an interdomain disulfide bond (Cys306 and Cys476) in each monomer, an extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) is identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates	Thermotoga maritima