|
|
|
|
|
Albenne, C.; Skov, L.K.; Mirza, O.; Gajhede, M.; Feller, G.; d'Amico, S.; André, G.; Potocki-Véronèse, G.; van der Veen, B.A.; Monsan, P.; Remaud-Simeon, M.. |
Amylosucrase from Neisseria polysaccharea is a remarkable transglucosidase from family 13 of the glycoside-hydrolases that synthesizes an insoluble amylose-like polymer from sucrose in the absence of any primer. Amylosucrase shares strong structural similarities with α-amylases. Exactly how this enzyme catalyzes the formation of α-1,4-glucan and which structural features are involved in this unique functionality existing in family 13 are important questions still not fully answered. Here, we provide evidence that amylosucrase initializes polymer formation by releasing, through sucrose hydrolysis, a glucose molecule that is subsequently used as the first acceptor molecule. Maltooligosaccharides of increasing size were produced and successively elongated at... |
Tipo: Journal Article |
Palavras-chave: AMYLOSUCRASE; EVOLUTION MOLECULAIRE DIRIGEE; ALPHA AMYLASE; AMYLOSACCHARASE; INGENIERIE ENZYMATIQUE; NEISSERIA POLYSACCHAREA; NEISSERIACEAE. |
Ano: 2004 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0500023786108456&uri=/notices/prodinra1/2010/11/ |
| |
|
|
Skov, L.K.; Mirza, O.; Henriksen, A.; Potocki de Montalk, G.; Remaud-Simeon, M.; Sarçabal, P.; Willemot, R.M.; Monsan, P.; Gajhede, M.. |
Amylosucrase (E.C. 2.4.1.4) is a member of Family 13 of the glycoside hydrolases (the α-amylases), although its biological function is the synthesis of amylose-like polymers from sucrose. The structure of amylosucrase from Neisseria polysaccharea is divided into five domains: an all helical N-terminal domain that is not similar to any known fold, a (β/α)8-barrel A-domain, B- and B′-domains displaying α/β-structure, and a C-terminal eight-stranded β-sheet domain. In contrast to other Family 13 hydrolases that have the active site in the bottom of a large cleft, the active site of amylosucrase is at the bottom of a pocket at the molecular surface. A substrate binding site resembling the amylase 2 subsite is not found in amylosucrase. The site is blocked by a... |
Tipo: Journal Article |
Palavras-chave: AMYLOSUCRASE; BACTERIE NON PATHOGENE; NEISSERIA POLYSACCHAREA; ALPHA AMYLASE; SACCHAROSE; STRUCTURE TRIDIMENSIONNELLE; GLYCOGENE; SEQUENCE NUCLEOTIDIQUE; ACTIVITE ENZYMATIQUE; GLYCOSIDE HYDROLYSE; NEISSERICEAE; BACTERIE GRAM NEGATIF; SUCRE. |
Ano: 2001 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400023316102157&uri=/notices/prodinra1/2010/10/ |
| |
|
|
|