Lin F, Marchenko G, Cheng Y R
Fujian Institute of Microbiology, PR, China.
J Ind Microbiol. 1994 Nov;13(6):344-50. doi: 10.1007/BF01577217.
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.
克隆了纤维素单孢菌86W-16的内切-β-1,4-葡聚糖酶基因mcenA，并测定了其核苷酸序列。发现一个1374个碱基的开放阅读框（ORF），编码一个由457个氨基酸组成、分子量为46742Da的肽（McenA）。它前面是革兰氏阳性型核糖体结合位点，后面是一个不完全反向重复序列。在McenA的N端有一个包含23个氨基酸的推定信号肽，在中部有一个拥有37个氨基酸的连接区。McenA的N端部分作为催化结构域，C端部分可能作为纤维素结合结构域（CBD）。删除后者并没有降低McenA的羧甲基纤维素酶活性。在McenA和来自双孢小双孢菌的内切葡聚糖酶MbcelA的氨基酸序列之间发现了显著的相似性（70%）。
