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Journal of Bacteriology, February 2008, p. 1375-1382, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01104-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of a New Rhamnogalacturonan Acetyl Esterase from Bacillus halodurans C-125 with a New Putative Carbohydrate Binding Domain{triangledown}

José Navarro-Fernández,1 Irene Martínez-Martínez,1 Silvia Montoro-García,1 Francisco García-Carmona,1 Hideto Takami,2 and Álvaro Sánchez-Ferrer1*

Department of Biochemistry and Molecular Biology-A, Faculty of Biology, University of Murcia, Campus Espinardo, E-30100 Murcia, Spain,1 Microbial Genome Research Group, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima, Yokosuka 237-0061, Japan2

Received 13 July 2007/ Accepted 30 November 2007

BH1115 is a gene from Bacillus halodurans strain C-125 that hypothetically encodes a rhamnogalacturonan acetyl esterase (RGAE) of the CE-12 family. As confirmation, this gene was cloned, and the product was expressed in Escherichia coli strain Rosetta (DE3) cells and purified. The enzyme obtained was monomeric, with a molecular mass of 45 kDa, and exhibited alkaliphilic properties. A study of the inhibition of the activity by some modulators confirmed that the catalytic triad for the esterase activity was Ser-His-Asp. This enzyme also presents broad substrate specificity and is active toward 7-aminocephalosporanic acid, cephalosporin C, p-nitrophenyl acetate, β-naphthyl acetate, glucose pentaacetate, and acetylated xylan. Moreover, RGAE from B. halodurans achieves a synergistic effect with xylanase A toward acetylated xylan. As a member of the SGNH family, it does not adopt the common {alpha}/β hydrolase fold. The homology between the folds of RGAE from Aspergillus aculeatus and the hypothetical YxiM precursor from Bacillus subtilis, which both belong to the SGNH family, illustrates the divergence of such proteins from a common ancestor. Furthermore, the enzyme possesses a putative substrate binding region at the N terminus of the protein which has never been described to date for any RGAE.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology-A, Faculty of Biology, University of Murcia, Campus Espinardo, E-30071 Murcia, Spain. Phone: 34968364770. Fax: 34968364147. E-mail: alvaro{at}um.es

{triangledown} Published ahead of print on 14 December 2007.

Journal of Bacteriology, February 2008, p. 1375-1382, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01104-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Montoro-Garcia, S., Martinez-Martinez, I., Navarro-Fernandez, J., Takami, H., Garcia-Carmona, F., Sanchez-Ferrer, A. (2009). Characterization of a Novel Thermostable Carboxylesterase from Geobacillus kaustophilus HTA426 Shows the Existence of a New Carboxylesterase Family. J. Bacteriol. 191: 3076-3085 [Abstract] [Full Text]  


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