Active-site structure of Rhizopus niveus glucoamylase.
نویسندگان
چکیده
منابع مشابه
The Rhizopus niveus glucoamylase-catalyzed reaction for substrate maltose in the absence or presence of acetonitrile
In the presence or absence of acetonitrile CH3CN, the molecular mechanism on the Rhizopus niveus glucoamylse (GA)-catalyzed reaction was studied by the steady-state kinetics for a substrate maltose (G2). At high concentration of G2, the GA-catalyzed reaction was observed not to obey the Michaelis kinetics and was reasonably explained with a mechanism of the substrate-inhibition involving the te...
متن کاملEvidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora
Arthrobotrysamerospora (ATCC 34468) produced glucoamylase in a semi-synthetic medium containing starch as a sole carbon source. Polyacrylamide gel electrophoresis of crude glucoamylase showed three isoenzymes. They were designated as glu I, glu II and glu III according to their electrophoretic mobility. These iso-glucoamylases were purified by column chromatography using DEAE-Sephadex A-50. The...
متن کاملSolution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase.
CBMs (carbohydrate-binding modules) function independently to assist carbohydrate-active enzymes. Family 21 CBMs contain approx. 100 amino acid residues, and some members have starchbinding functions or glycogen-binding activities. We report here the first structure of a family 21 CBM from the SBD (starch-binding domain) of Rhizopus oryzae glucoamylase (RoCBM21) determined by NMR spectroscopy. ...
متن کاملevidence of tryptophan at or near active site of glucoamylase i of arthrobotrys amerospora
arthrobotrysamerospora (atcc 34468) produced glucoamylase in a semi-synthetic medium containing starch as a sole carbon source. polyacrylamide gel electrophoresis of crude glucoamylase showed three isoenzymes. they were designated as glu i, glu ii and glu iii according to their electrophoretic mobility. these iso-glucoamylases were purified by column chromatography using deae-sephadex a-50. the...
متن کاملAutomated Docking of α-(1,4)- and α-(1,6)-Linked Glucosyl Trisaccharides in the Glucoamylase Active Site
Low-energy conformers of five α-(1,4)and α-(1,6)-linked glucosyl trisaccharides were flexibly docked into the glucoamylase active site using AutoDock 2.2. To ensure that all significant conformational space was searched, the starting trisaccharide conformers for docking were all possible combinations of the corresponding disaccharide low-energy conformers. All docked trisaccharides occupied sub...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of the Japanese Society of Starch Science
سال: 1987
ISSN: 1884-488X,0021-5406
DOI: 10.5458/jag1972.34.58