Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus
| Autor: | Moreland D. Gibbs, R. H. Mchale, Peter L. Bergquist, Greg D Albertson |
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| Rok vydání: | 1997 |
| Předmět: |
Glycoside Hydrolases
Molecular Sequence Data Biophysics Biology medicine.disease_cause Biochemistry Bacteria Anaerobic Open Reading Frames Structural Biology Enzyme Stability Genetics medicine Amino Acid Sequence Cloning Molecular Pullulanase activity Escherichia coli Peptide sequence Thermostability Sequence Homology Amino Acid Pullulanase Thermophile biology.organism_classification Open reading frame Caldicellulosiruptor saccharolyticus |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1354:35-39 |
| ISSN: | 0167-4781 |
| DOI: | 10.1016/s0167-4781(97)00123-1 |
| Popis: | A gene coding for a pullulanase from the obligately anaerobic, extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus has been cloned in Escherichia coli. It consists of an open reading frame (pulA) of 2478 bp which codes for an enzyme of 95 732 Da and is flanked by two other open reading frames. A truncated version of the gene which lacks 381 bp of 5′-sequence also has pullulanase activity and it appears that the amino-terminal portion of the gene is not essential for either activity or thermostability. Amino acid sequence comparisons with other published amylases and pullulanases showed that it possesses homology to the four key regions common to these enzymes. |
| Databáze: | OpenAIRE |
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