Identification of a gene coding fora deglycosylating enzyme in Hypocrea jecorina

被引：54

作者：

Stals, Ingeborg ^{[1
,2
]}

Samyn, Bart ^{[2
]}

Sergeant, Kjell ^{[2
]}

White, Theresa ^{[3
]}

Hoorelbeke, Katleen ^{[1
,2
]}

Coorevits, An ^{[1
,2
]}

Devreese, Bart ^{[2
]}

Claeyssens, Marc ^{[2
]}

Piens, Kathleen ^{[2
]}

机构：

[1] Univ Coll Ghent, Fac Appl Engn Sci, B-9000 Ghent, Belgium

[2] Univ Ghent, Dept Biochem & Microbiol, Lab Prot Biochem & Biomol Engn, B-9000 Ghent, Belgium

[3] Iogen Corp, Ottawa, ON, Canada

来源：

FEMS MICROBIOLOGY LETTERS | 2010年 / 303卷 / 01期

关键词：

endo-N-acetyl-beta-D-glucosaminidase; deglycosylation; Hypocrea jecorina; Trichoderma reesei; GH family 18; EC; 3.2.1.96; BETA-N-ACETYLGLUCOSAMINIDASE; FUNGUS TRICHODERMA-REESEI; FACTORS INFLUENCING GLYCOSYLATION; CELLOBIOHYDROLASE-I; MOLECULAR-CLONING; SEQUENCE-ANALYSIS; CELLULASES; PROTEIN; ELECTROPHORESIS; PHYLOGENY;

D O I：

10.1111/j.1574-6968.2009.01849.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

An enzyme with mannosyl glycoprotein endo-N-acetyl-beta-D-glucosaminidase (ENGase)-type activity was partially purified from the extracellular medium of the mould Hypocrea jecorina (Trichoderma reesei). Internal peptides were generated and used to identify the gene in the T. reesei genome. The active enzyme is processed both at the N- and at the C-terminus. High-mannose-type glycoproteins are good substrates, whereas complex-type glycans are not hydrolysed. The enzyme represents the first fungal member of glycoside hydrolase family 18 with ENGase-type activity. Bacterial ENGases and the fungal chitinases belonging to the same family show very low homology with Endo T. Database searches identify several highly homologous genes in fungi and the activity is also found within other Trichoderma species. This ENGase activity, not coregulated with cellulase production, could be responsible for the extensive N-deglycosylation observed for several T. reesei cellulases.

引用

页码：9 / 17

页数：9

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