F. Lin et al., CLONING AND SEQUENCING OF AN ENDO-BETA-1,4-GLUCANASE GENE MCENA FROM MICROMONOSPORA-CELLULOLYTICUM 86W-16, Journal of industrial microbiology, 13(6), 1994, pp. 344-350
Endo-beta-1,4-glucanase gene mcenA of Micromonospora cellulolyticum 86
W-16 was cloned, and the nucleotide sequence was determined. An open r
eading 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 re
peat. A putative signal peptide containing 23 amino acids is at the N-
terminus and a linker region possessing 37 amino acids is in the midpa
rt of McenA. The N-half of McenA functions as the catalytic domain and
the C-half might serve as a cellulose-binding domain (CBD). Deletion
of the latter did not decrease the CMCase activity of McenA. Significa
nt similarity (70%) was found between the amino acid sequences of Mcen
A and MbcelA, an endoglucanase from Microbispora bispora.