CelF of Orpinomyces PC-2 has an intron and encodes a cellulase (CelF) containing a carbohydrate-binding module

A cDNA, designated celF, encoding a cellulase (CelF) was isolated from the anaerobic fungus Orpinomyces PC-2. The open reading frame contains regions coding for a signal peptide, a carbohydrate-binding module (CBM), a linker, and a catalytic domain. The catalytic domain was homologous to those of Ce...

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Veröffentlicht in:Applied biochemistry and biotechnology 2003, Vol.105 -108 (1-3), p.775-785
Hauptverfasser: Chen, Huizhong, Li, Xin-Liang, Blum, David L, Ximenes, Eduardo A, Ljungdahl, Lars G
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Sprache:eng
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Zusammenfassung:A cDNA, designated celF, encoding a cellulase (CelF) was isolated from the anaerobic fungus Orpinomyces PC-2. The open reading frame contains regions coding for a signal peptide, a carbohydrate-binding module (CBM), a linker, and a catalytic domain. The catalytic domain was homologous to those of CelA and CelC of the same fungus and to that of the Neocallimastix patriciarum CELA, but CelF lacks a docking domain, characteristic for enzymes of cellulosomes. It was also homologous to the cellobiohydrolase IIs and endoglucanases of aerobic organisms. The gene has a 111-bp intron, located within the CBM-coding region. Some biochemical properties of the purified recombinant enzyme are described.
ISSN:0273-2289
0273-2289
1559-0291
DOI:10.1385/ABAB:108:1-3:775