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Journal of Bacteriology, May 2002, p. 2399-2403, Vol. 184, No. 9
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.9.2399-2403.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Novel Carbohydrate-Binding Module of ß-1,3-Xylanase from a Marine Bacterium, Alcaligenes sp. Strain XY-234

Fumiyoshi Okazaki,¹ Yutaka Tamaru,¹ Shinnosuke Hashikawa,^1, Yu-Teh Li,² and Toshiyoshi Araki^1*

Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, Mie 514-8507, Japan,¹ Department of Biochemistry, Tulane University School of Medicine, New Orleans, Louisiana 70112²

Received 21 August 2001/ Accepted 7 February 2002

A ß-1,3-xylanase gene (txyA) from a marine bacterium, Alcaligenes sp. strain XY-234, has been cloned and sequenced. txyA consists of a 1,410-bp open reading frame that encodes 469 amino acid residues with a calculated molecular mass of 52,256 Da. The domain structure of the ß-1,3-xylanase (TxyA) consists of a signal peptide of 22 amino acid residues, followed by a catalytic domain which belongs to family 26 of the glycosyl hydrolases, a linker region with one array of DGG and six repeats of DNGG, and a novel carbohydrate-binding module (CBM) at the C terminus. The recombinant TxyA hydrolyzed ß-1,3-xylan but not other polysaccharides such as ß-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan, or ß-1,4-mannan. TxyA was capable of binding specifically to ß-1,3-xylan. The analysis using truncated TxyA lacking either the N- or C-terminal region indicated that the region encoding the CBM was located between residues 376 and 469. Binding studies on the CBM revealed that the K_d and the maximum amount of protein bound to ß-1,3-xylan were 4.2 µM and 18.2 µmol/g of ß-1,3-xylan, respectively. Furthermore, comparison of the enzymatic properties between proteins with and without the CBM strongly indicated that the CBM of TxyA plays an important role in the hydrolysis of ß-1,3-xylan.

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* Corresponding author. Mailing address: Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, Mie 514-8507, Japan. Phone: 81-59-231-9561. Fax: 81-59-231-9557. E-mail: araki{at}bio.mie-u.ac.jp.

Present address: Department of Microbiology, Graduate School of Medicine, Nagoya University, 65 Tsurumai, Showa, Nagoya, Aichi 466-8550, Japan.

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Journal of Bacteriology, May 2002, p. 2399-2403, Vol. 184, No. 9
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.9.2399-2403.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

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