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Cloning and sequencing of an endo-β-1,4-glucanase genemcenA fromMicromonospora cellulolyticum 86W-16

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Journal of Industrial Microbiology

Summary

Endo-β-1,4-glucanase genemcenA ofMicromonospora cellulolyticum 86W-16 was cloned, and the nucleotide sequence was determined. An open reading frame (ORF) of 1374 bases, coding for a peptide (McenA) of 457 amino acids and 46742 Da, was found. It is preceded by a Gram-positive type of ribosomebinding site and followed by an imperfect inverted repeat. A putative signal peptide containing 23 amino acids is at the N-terminus and a linker region possessing 37 amino acids is in the midpart of McenA. The N-half of McenA functions as the catalytic domain and the C-half might serve as a cellulosebinding domain (CBD). Deletion of the latter did not decrease the CMCase activity of McenA. Significant similarity (70%) was found between the amino acid sequences of McenA and MbcelA, an endoglucanase fromMicrobispora bispora.

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Lin, F., Marchenko, G. & Cheng, YR. Cloning and sequencing of an endo-β-1,4-glucanase genemcenA fromMicromonospora cellulolyticum 86W-16. Journal of Industrial Microbiology 13, 344–350 (1994). https://doi.org/10.1007/BF01577217

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  • DOI: https://doi.org/10.1007/BF01577217

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