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| 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/ |
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