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Amylosucrase, a glucan-synthesizing enzyme from the α-amylase family Inra
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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Identification of differentially expressed genes in chickens differing in muscle glycogen content and meat quality. Inra
Sibut, V.; Hennequet-Antier, C.; Le Bihan-Duval, E.; Marthey, S.; Duclos, M.J.; Berri, C..
Tipo: Journal Article Palavras-chave: GLYCOGENE; MICROARRAY.
Ano: 2011 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201187c39f5b&uri=/notices/prodinra1/2011/03/
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Structure, fatigue, and enzyme activities in "fast" insect muscles National Institute of Agronomic Research
Smit, W.A.; Becht, G.; Beenakkers, A.M.Th..
Two groups of extensores trochanteris of the mesothoracic leg of Periplaneta americana were investigated: (1) the main depressor of the leg, which is also a flight muscle; (2) the coxal depressor of the leg. These muscle groups are known to be equally ‘fast’ in mechanical and electrical responses. The group used for walking as well as for flying has the greatest endurance. This is correlated with a larger number of sarcosomes, more glycogen, a better oxygensupply, a higher activity of some energy-supplying enzymes, and a structural difference of neuromuscular junctions.
Tipo: Journal Article-postprint Palavras-chave: PERIPLANETA AMERICANA; MESOTHORACIC LEG; MUSCLE; FLIGHT MUSCLE; STRUCTURE; NEUROMUSCULAR JUNCTION; MECHANICAL RESPONSE; ELECTRICAL RESPONSE; SARCOSOME; GLYCOGEN; OXYGEN SUPPLY; ENERGY; ENZYME; PERIPLANETA AMERICANA; PATTE MESOTHORACIQUE; MUSCLE ALAIRE; SARCOSOME; GLYCOGENE; OXYGENE; ENERGIE; ENZYME; STRUCTURE; JONCTION NEUROMUSCULAIRE; REPONSE MECANIQUE; ELECTRICITE.
Ano: 1967 URL: http://hdl.handle.net/2174/377
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