scholarly journals Evidence for a single active site on sugar beet .ALPHA.-glucosidase with maltase and glucoamylase activities.

1981 ◽  
Vol 45 (1) ◽  
pp. 141-147 ◽  
Author(s):  
Hirokazu MATSUI ◽  
Seiya CHIBA
Keyword(s):  
Sugar Beet ◽  
Active Site ◽  
Alpha Glucosidase

scholarly journals Purification and properties of an .ALPHA.-glucosidase (glucoamylase) in sugar beet seed.

1978 ◽  
Vol 42 (2) ◽  
pp. 241-245 ◽  
Author(s):  
Seiya CHIBA ◽  
Seizo INOMATA ◽  
Hirokazu MATSUI ◽  
Tokuji SHIMOMURA
Keyword(s):  
Sugar Beet ◽  
Purification And Properties ◽  
Alpha Glucosidase

scholarly journals Docking Molekular dari Trigonella foenum- graceum sebagai Antidiabetes menggunakan molegro virtual docking.

2020 ◽  
Vol 4 (2) ◽  
Author(s):  
Andri Prasetiyo Prasetiyo
Keyword(s):  
Sugar Beet ◽  
In Silico ◽  
Dipeptidyl Peptidase ◽  
Peroxisome Proliferator ◽  
Dipeptidyl Peptidase 4 ◽  
Alpha Glucosidase

Trigonella foenum-graceum atau fenugreek digunakan secara luas  sebagai obat tradisional  untuk pengobatan diabetes tetapi mekanisme kerjanya masih belum jelas. Penelitian bertujuan memprediksi senyawa dalam fenugreek yang berkhasiat sebagai antidiabetes secara in-silico dengan menggunakan perangkat lunak Molegro Virtual Docking . Docking dilakukan 10 Senyawa uji dalam fenugreek yaitu 4-hidroxyisoleucine, coumarine, diosgenin, galactomannan, isovitexin, quarcetin, tigogenin, trigoneline, vitexin dan yamogenin dengan 3 reseptor yaitu sugar beet alpha-glucosidase- (PDB ID : 3W37), human dipeptidyl peptidase-4 (PDB ID : 2RGU), human peroxisome proliferator activated gamma (PDB: 2PRG) serta senyawa pembanding acarbose, linagliptin dan rosiglitazone. Dari 10 senyawa uji, galactomanann  memiliki nilai Rerank Score/RS paling rendah di dua reseptor yaitu alpha glucosidase dan peroxisome proliferator activated gamma dengan nilai berturut turut -116,558kkal/mol dan -131.184kkal/mol dan nilai RS acarbose -113.595kkal/mol dan rosiglitazone -124.537kkal/mol . Dari 10 senyawa uji, vitexin memiliki nilai RS paling rendah direseptor dipeptidyl peptidase-4 dengan nilai RS -86.7288 kkal/mol dan nilai RS linagliptin 109.665kkal/mol. Berdasarkan nilai RS, galactomannan diprediksi memiliki aktivitas antidiabetes yang bekerja pada reseptor alpha-glucosidase dan peroxisome proliferator activated gamma sedangkan vitexin diprediksi memiliki aktivitas antidiabetes yang bekerja pada reseptor dipeptidyl peptidase-4.

scholarly journals Extracellular .ALPHA.-Glucosidase from Suspension-cultured Sugar-beet Cells.

1991 ◽  
Vol 55 (6) ◽  
pp. 1675-1676 ◽  
Author(s):  
Yoshiki YAMASAKI ◽  
Haruyoshi KONNO
Keyword(s):  
Sugar Beet ◽  
Alpha Glucosidase

scholarly journals Substrate specificity of an .ALPHA.-glucosidase in sugar beet seed.

1978 ◽  
Vol 42 (10) ◽  
pp. 1855-1860 ◽  
Author(s):  
Hirokazu MATSUI ◽  
Seiya CHIBA ◽  
Tokuji SHIMOMURA
Keyword(s):  
Sugar Beet ◽  
Substrate Specificity ◽  
Alpha Glucosidase

scholarly journals Kinetic studies on the active site of pig serum .ALPHA.-glucosidase and buckwheat .ALPHA.-glucosidase.

1977 ◽  
Vol 41 (7) ◽  
pp. 1245-1248 ◽  
Author(s):  
Seiya CHIBA ◽  
Nozomu HIBI ◽  
Ken-ichi KANAYA ◽  
Tokuji SHIMOMURA
Keyword(s):  
Active Site ◽  
Kinetic Studies ◽  
Alpha Glucosidase ◽  
Pig Serum

scholarly journals Dynamical origins of heat capacity changes in enzyme catalysed reactions

2017 ◽  
Author(s):  
Marc W van der Kamp ◽  
Erica J. Prentice ◽  
Kirsty L. Kraakmann ◽  
Michael Connolly ◽  
Adrian J. Mulholland ◽  
...  
Keyword(s):  
Heat Capacity ◽  
Active Site ◽  
Reaction Rates ◽  
Heat Capacity Change ◽  
Catalysed Reaction ◽  
Capacity Change ◽  
Heat Capacity Changes ◽  
Dynamics Simulations ◽  
Alpha Glucosidase ◽  
Activation Heat

AbstractHeat capacity changes are emerging as essential for explaining the temperature dependence of enzyme-catalysed reaction rates. This has important implications for enzyme kinetics, thermoadaptation and evolution, but the physical basis of these heat capacity changes is unknown. Here we show by a combination of experiment and simulation, for two quite distinct enzymes (dimeric ketosteroid isomerase and monomeric alpha-glucosidase), that the activation heat capacity change for the catalysed reaction can be predicted through atomistic molecular dynamics simulations. The simulations reveal subtle and surprising underlying dynamical changes: tightening of loops around the active site is observed as expected, but crucially, changes in energetic fluctuations are evident across the whole enzyme including important contributions from oligomeric neighbours and domains distal to the active site. This has general implications for understanding enzyme catalysis and demonstrating a direct connection between functionally important microscopic dynamics and macroscopically measurable quantities.

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