Structure and function of protein domains from thermostable beta-glucanases

Informations projet

N° de convention de subvention: INTAS-94-1328

Projet clôturé

Date de début 1 Juin 1995

Date de fin 31 Mai 1998

Financé au titre de

• International Association for the promotion of cooperation with scientists from the independent states of the former Soviet Union (INTAS), 1993-

Coût total

Aucune donnée

Contribution de l’UE

€ 38 000,00

Coordonné par

Technische Universität München
Germany

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Résultats exploitables

Structure and function of protein domains from thermostable b-glucanases

The lamA gene from Thermotoga neapolitana was cloned and sequenced. It consists of a catalytic domain flanked by two non-catalytic domains, possibly mediating binding to β-1,3-glucan. It is one of the most thermostable β-1,3-glucanase known to date. Its gene is preceded by the β-glucosidase gene bglB, possibly functioning as a co-regulated operon. The BglB protein is a β-1,3-glucosidase (laminaribiase) and together with LamA completely hydrolyses β-1,3-glucan to glucose monomers. Thermotoga strains possess two β-glucosidases genes, which are expressed. They belong to different glycosyl hydrolases families (1 and 3). In contrast to β-1,4-glucanase genes, no genes for β-1,3-glucanases could be identified in Anaerocellum thermophilium. A publicly accessible server was set up (CAZY) where all hitherto known protein moduls identified in glycosyl hydrolases can be browsed. Each entry is linked to different data bases.