%0 Journal Article
%T Cloning and characterization of full-length cDNA of chitinase gene from Isaria farinosa<br>粉棒束孢几丁质酶基因cDNA全序列克隆及结构特征分析
%A HUANG Bo
%A ZHANG Zhong
%A PENG Fan
%A FAN Mei-Zhen
%A LI Zeng-Zhi
%A <br>黄勃
%A 张中
%A 彭凡
%A 樊美珍
%A 李增智
%J 菌物学报
%D 2006
%I 
%X The full-length cDNA coding the chitinases produced by the biocontrol agent Isaria farinosa using SMART RACE RT-PCR was reported in this paper. Analysis of the cloned complete cDNA, with a whole sequence of 1549bp, showed that it encompassed an open reading frame (ORF) of 1272bp encoding 423 amino acids with a stretch of 22 amino acid residues displaying characteristics of signal peptide. The result showed that the mature chitinase (without signal sequence) had a molecular mass of 43.9 kDa with a calculated pI of 5.67. This sequence contained two highly conserved regions of the active domain of the family 18 glycosyl hydrolases including a presumed enzymatic active site and a potential chitin-binding domain. The cloned Isaria chinitase belongs to the class V in 18 family of glycosyl hydrolase. Alignments with the deduced amino acid of mature proteins in 5 species of fungi showed 91%, 89%, 80%, 76% and 75%, respectively, identical with those of Torrubiella confragosa (AAV98691), Aphanocladium album (CAA45468), Verticillium fungicola (AAP45631), Nomuraea rileyi (AAP04616) and Beauveria bassiana (AAN41261), respectively.
%K Entomogenous fungi
%K Extracellular enzyme
%K Paecilomyces farinosus<br>虫生真菌
%K 胞外分泌酶
%K 粉拟青霉
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=CA9F815FCB0F62294C4266BB6F902ACB&aid=01D940F43AF7E75A&yid=37904DC365DD7266&vid=C5154311167311FE&iid=E158A972A605785F&sid=06F643376BC2509E&eid=50B6AC44200581A5&journal_id=1672-6472&journal_name=菌物学报&referenced_num=0&reference_num=22