Cloning and sequencing of an endo-beta-1,4-glucanase gene mcenA from Micromonospora cellulolyticum 86W-16.
Endo-beta-1,4-glucanase gene mcenA of Micromonospora 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 46,742 Da, was found. It is preceded by a Gram-positive type of ribosome-binding 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 cellulose-binding 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 from Microbispora bispora.
Lin
F
F
Fujian Institute of Microbiology, PR, China.
Marchenko
G
G
Cheng
Y R
YR
D000595:Amino Acid Sequence; D001483:Base Sequence; D002480:Cellulase / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics*; D008847:Micromonospora / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D002480:Cellulase