Literature summary for 3.2.1.8 extracted from

Natesh, R.; Bhanumoorthy, P.; Vithayathil, P.J.; Sekar, K.; Ramakumar, S.; Viswamitra, M.A.
Crystal structure at 1.8 A resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus (1999), J. Mol. Biol., 288, 999-1012 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.8 A resolution. The active site consists of two glutamate residues located at the C-terminus end of the beta-barrel, conforming to the double displacement mechanism for the enzyme action. A disulfide bond and more than ten salt bridges are present. The salt bridge Arg124-Glu232, which is almost buried, bridges the beta-strands b4 and b7 where the catalytic glutamate residues reside, and may play a key role in the stability and activity at elevated temperature. A proline residue in the middle of the alpha-helix a6 may be contributing to better packing	Thermoascus aurantiacus

Crystallization (Comment)

Organism

to 1.8 A resolution. The active site consists of two glutamate residues located at the C-terminus end of the beta-barrel, conforming to the double displacement mechanism for the enzyme action. A disulfide bond and more than ten salt bridges are present. The salt bridge Arg124-Glu232, which is almost buried, bridges the beta-strands b4 and b7 where the catalytic glutamate residues reside, and may play a key role in the stability and activity at elevated temperature. A proline residue in the middle of the alpha-helix a6 may be contributing to better packing

Thermoascus aurantiacus

Organism

Organism	UniProt	Comment	Textmining
Thermoascus aurantiacus	P23360	-	-

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Release 2023.1 (January 2023)