Porcine pancreatic α-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (α-AI1) and structural changes in the α-amylase inhibitor complex

Autor: Roger Koukiekolo, Guy Marchis-Mouren, Marius Santimone, Véronique Le Berre, Véronique Desseaux, Pierre Rougé, Yann Moreau

Publikováno v: Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2004, 1696 (2), pp.181-190. ⟨10.1016/j.bbapap.2003.11.001⟩
Biochimica et Biophysica Acta Proteins and Proteomics, 2004, 1696 (2), pp.181-190. ⟨10.1016/j.bbapap.2003.11.001⟩

Porcine pancreatic alpha-amylase (PPA) is inhibited by the red kidney bean (Phaseolus vulgaris) inhibitor alpha-AI1 [Eur. J. Biochem. 265 (1999) 20]. Inhibition kinetics were carried out using DP 4900-amylose and maltopentaose as substrate. As shown

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc40e7d1ab229745a24f02ca3d5e4b47
https://doi.org/10.1016/j.bbapap.2003.11.001

Isolation, characterization and inhibition by acarbose of the α-amylase from Lactobacillus fermentum: comparison with Lb. manihotivorans and Lb. plantarum amylases

Autor: Yann Moreau, Guy Marchis-Mouren, Véronique Desseaux, Marius Santimone, P Talamond

Publikováno v: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 133:351-360

Extracellular alpha-amylase from Lactobacillus fermentum (FERMENTA) was purified by glycogen precipitation and ion exchange chromatography. The purification was approximately 28-fold with a 27% yield. The FERMENTA molecular mass (106,000 Da) is in th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eba1d859c66f2623f944cdf171cbfb93
https://doi.org/10.1016/s1096-4959(02)00157-4

Mechanism of porcine pancreatic α-amylase

Autor: Marius Santimone, Guy Marchis-Mouren, Véronique Desseaux, Yann Moreau, Roger Koukiekolo

Publikováno v: European Journal of Biochemistry. 268:841-848

The effects of alpha-, beta- and gamma-cyclodextrins on the amylose and maltopentaose hydrolysis catalysed by porcine pancreatic alpha-amylase (PPA) were investigated. The results of the statistical analysis performed on the kinetic data using the ge

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2f5abc9e1999c76d747447de9f79d25
https://doi.org/10.1046/j.1432-1327.2001.01950.x

Inhibition of reduced DP18-maltodextrin and amylose hydrolysis by acarbose: kinetic studies

Autor: Modhafar Alkazaz, Véronique Desseaux, Marius Santimone, Eugenio Prodanov, Guy Marchis-Mouren

Publikováno v: International Journal of Biological Macromolecules. 21:97-101

Kinetics of inhibition of porcine pancreatic alpha-amylase by acarbose were performed using maltodextrin and amylose as substrates. Similar Lineweaver-Burk primary plots were obtained. Two mixed non-competitive models are proposed. X-ray crystallogra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60dcc597097ab3186d16a728e6e510d3
https://doi.org/10.1016/s0141-8130(97)00047-0

Crystal Structure of Pig Pancreatic alpha-amylase Isoenzyme II, in Complex with the Carbohydrate Inhibitor Acarbose

Autor: Christian Cambillau, Guy Marchis-Mouren, Françoise Payan, Jean-Pierre Astier, Coralie Gilles

Publikováno v: European Journal of Biochemistry. 238:561-569

Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have been compared together and to previously reported structures of PPAI. A crystal form obtained at 4 degre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d40a993fdd382a4e6a7e760287416d66
https://doi.org/10.1111/j.1432-1033.1996.0561z.x