This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jindou, S.
Right arrow Articles by Ohmiya, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jindou, S.
Right arrow Articles by Ohmiya, K.
Right arrowPubmed/NCBI databases
*Protein
*Compound via MeSH
*Substance via MeSH
*Genetics Home Reference

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2002, p. 600-604, Vol. 184, No. 2
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.2.600-604.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

{alpha}-Galactosidase Aga27A, an Enzymatic Component of the Clostridium josui Cellulosome

Sadanari Jindou,1 Shuichi Karita,1 Emi Fujino,1 Tsuchiyoshi Fujino,2 Hidenori Hayashi,1 Tetsuya Kimura,1 Kazuo Sakka,1* and Kunio Ohmiya1

Faculty of Bioresources, Mie University, Tsu 514-8507, Japan,1 Nagoya Seiraku Co. Ltd., Nagoya 468-8588, Japan2

Received 2 July 2001/ Accepted 17 October 2001

The Clostridium josui aga27A gene encodes the cellulosomal {alpha}-galactosidase Aga27A, which comprises a catalytic domain of family 27 of glycoside hydrolases and a dockerin domain responsible for cellulosome assembly. The catalytic domain is highly homologous to those of various {alpha}-galactosidases of family 27 of glycoside hydrolases from eukaryotic organisms, especially plants. The recombinant Aga27A {alpha}-galactosidase devoid of the dockerin domain preferred highly polymeric galactomannan as a substrate to small saccharides such as melibiose and raffinose.


* Corresponding author. Mailing address: Faculty of Bioresources, Mie University, 1515 Kamihamacho, Tsu 514-8507, Japan. Phone: (81) 59-231-9621. Fax: (81) 59-231-9684. E-mail: sakka{at}bio.mie-u.ac.jp.


Journal of Bacteriology, January 2002, p. 600-604, Vol. 184, No. 2
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.2.600-604.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Blouzard, J.-C., Bourgeois, C., de Philip, P., Valette, O., Belaich, A., Tardif, C., Belaich, J.-P., Pages, S. (2007). Enzyme Diversity of the Cellulolytic System Produced by Clostridium cellulolyticum Explored by Two-Dimensional Analysis: Identification of Seven Genes Encoding New Dockerin-Containing Proteins. J. Bacteriol. 189: 2300-2309 [Abstract] [Full Text]  
  • Jindou, S., Soda, A., Karita, S., Kajino, T., Beguin, P., Wu, J. H. D., Inagaki, M., Kimura, T., Sakka, K., Ohmiya, K. (2004). Cohesin-Dockerin Interactions within and between Clostridium josui and Clostridium thermocellum: BINDING SELECTIVITY BETWEEN COGNATE DOCKERIN AND COHESIN DOMAINS AND SPECIES SPECIFICITY. J. Biol. Chem. 279: 9867-9874 [Abstract] [Full Text]  
  • Han, S. O., Yukawa, H., Inui, M., Doi, R. H. (2003). Regulation of Expression of Cellulosomal Cellulase and Hemicellulase Genes in Clostridium cellulovorans. J. Bacteriol. 185: 6067-6075 [Abstract] [Full Text]  
  • Han, S. O., Yukawa, H., Inui, M., Doi, R. H. (2003). Transcription of Clostridium cellulovorans Cellulosomal Cellulase and Hemicellulase Genes. J. Bacteriol. 185: 2520-2527 [Abstract] [Full Text]