serine and isomaltose

serine has been researched along with isomaltose in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Coutinho, PM; Fang, TY; Ford, C; Reilly, PJ	1
Hemmi, H; Inohara-Ochiai, M; Min, KS; Nakayama, T; Nishino, T; Noguchi, A; Ohshima, Y; Okada, M; Yano, M	1

Other Studies

2 other study(ies) available for serine and isomaltose

Article	Year
Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48Phe49-->Trp, Tyr116-->Trp, Tyr175-->Phe, Arg241-->Lys, Ser411-->Ala and Ser411-->Gly. Protein engineering, 1998, Volume: 11, Issue:2 Topics: Arginine; Aspergillus; Binding Sites; Carbohydrate Conformation; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucose; Hydrolysis; Isomaltose; Kinetics; Molecular Structure; Mutagenesis, Site-Directed; Polysaccharides; Serine; Structure-Activity Relationship; Thermodynamics; Tyrosine	1998
Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606. Journal of biochemistry, 2003, Volume: 134, Issue:4 Topics: alpha-Glucosidases; Amino Acid Sequence; Amino Acids; Asparagine; Bacillus; Binding Sites; Catalysis; Evolution, Molecular; Glycine; Isomaltose; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Oligo-1,6-Glucosidase; Phylogeny; Plasmids; Proline; Serine; Substrate Specificity; Threonine; Trehalose	2003

Article

Year

Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48Phe49-->Trp, Tyr116-->Trp, Tyr175-->Phe, Arg241-->Lys, Ser411-->Ala and Ser411-->Gly.

Protein engineering, 1998, Volume: 11, Issue:2

Topics: Arginine; Aspergillus; Binding Sites; Carbohydrate Conformation; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucose; Hydrolysis; Isomaltose; Kinetics; Molecular Structure; Mutagenesis, Site-Directed; Polysaccharides; Serine; Structure-Activity Relationship; Thermodynamics; Tyrosine

1998

Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606.

Journal of biochemistry, 2003, Volume: 134, Issue:4

Topics: alpha-Glucosidases; Amino Acid Sequence; Amino Acids; Asparagine; Bacillus; Binding Sites; Catalysis; Evolution, Molecular; Glycine; Isomaltose; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Oligo-1,6-Glucosidase; Phylogeny; Plasmids; Proline; Serine; Substrate Specificity; Threonine; Trehalose

2003