caa a22 4500 475746031 CHVBK 20180406123513.0 cr unu---uuuuu 170329e20000501xx s 000 0 eng 10.1007/s002849910066 doi (NATIONALLICENCE)springer-10.1007/s002849910066 Multidomain and Multifunctional Glycosyl Hydrolases from the Extreme Thermophile Caldicellulosiruptor Isolate Tok7B.1 [Elektronische Daten] [Moreland D. Gibbs, Rosalind A. Reeves, G. King Farrington, Paige Anderson, Diane P. Williams, Peter L. Bergquist] Abstract.: DNA sequencing techniques have revealed widespread molecular diversity of the genomic organization of apparently closely related bacteria (as judged from SSU rDNA sequence similarity). We have previously described the extreme thermophile Caldicellulosiruptor saccharolyticus, which is unusual in possessing multi-catalytic, multidomain arrangements for the majority of its glycosyl hydrolases. We report here the sequencing of three gene clusters of glycosyl hydrolases from Caldicellulosiruptor sp. strain Tok7B.1. These clusters are not closely linked, and each is different in its organization from any described for Cs. saccharolyticus. The catalytic domains of the enzymes belong to glycosyl hydrolase families 5, 9, 10, 43, 44, and 48. The cellulose binding domains (CBDs) of these enzymes from Caldicellulosiruptor sp. Tok7B.1 are types IIIb, IIIc, or VI. A number of individual catalytic and binding domains have been expressed in Escherichia coli, and biochemical data are reported on the purified enzymes for cellulose degradation encoded by engineered derivatives of celB and celE. Springer-Verlag New York Inc., 2000 Gibbs Moreland D. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut Reeves Rosalind A. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut Farrington G. King Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut Anderson Paige Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut Williams Diane P. Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut Bergquist Peter L. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut https://doi.org/10.1007/s002849910066 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s002849910066 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gibbs Moreland D. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut NATIONALLICENCE 700 1- Reeves Rosalind A. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut NATIONALLICENCE 700 1- Farrington G. King Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut NATIONALLICENCE 700 1- Anderson Paige Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut NATIONALLICENCE 700 1- Williams Diane P. Clariant Corporation, Biotech Research Division, Lexington, MA 02173, USA, US aut NATIONALLICENCE 700 1- Bergquist Peter L. Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia, AU aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer