Page last updated: 2024-08-17

lysine and adenosine 3'-phosphate-5'-phosphate

lysine has been researched along with adenosine 3'-phosphate-5'-phosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hsiao, YS; Yang, YS	1
Fuda, H; Lee, KA; Lee, YC; Negishi, M; Pedersen, LC; Strott, CA	1

Other Studies

2 other study(ies) available for lysine and adenosine 3'-phosphate-5'-phosphate

Article	Year
A single mutation converts the nucleotide specificity of phenol sulfotransferase from PAP to AMP. Biochemistry, 2002, Oct-29, Volume: 41, Issue:43 Topics: Adenosine Diphosphate; Adenosine Monophosphate; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Arylsulfotransferase; Binding Sites; Humans; Lysine; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Rats; Recombinant Proteins; Sequence Alignment; Serine; Substrate Specificity	2002
Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. The Journal of biological chemistry, 2003, Nov-07, Volume: 278, Issue:45 Topics: Adenosine Diphosphate; Aspartic Acid; Binding Sites; Cholesterol; Crystallization; Crystallography, X-Ray; Dehydroepiandrosterone; Escherichia coli; Gene Expression; Humans; Hydrogen Bonding; Isoenzymes; Lysine; Models, Molecular; Molecular Structure; Pregnenolone; Protein Structure, Secondary; Recombinant Fusion Proteins; Substrate Specificity; Sulfotransferases; Transfection	2003

Article

Year

A single mutation converts the nucleotide specificity of phenol sulfotransferase from PAP to AMP.

Biochemistry, 2002, Oct-29, Volume: 41, Issue:43

Topics: Adenosine Diphosphate; Adenosine Monophosphate; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Arylsulfotransferase; Binding Sites; Humans; Lysine; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Rats; Recombinant Proteins; Sequence Alignment; Serine; Substrate Specificity

2002

Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms.

The Journal of biological chemistry, 2003, Nov-07, Volume: 278, Issue:45

Topics: Adenosine Diphosphate; Aspartic Acid; Binding Sites; Cholesterol; Crystallization; Crystallography, X-Ray; Dehydroepiandrosterone; Escherichia coli; Gene Expression; Humans; Hydrogen Bonding; Isoenzymes; Lysine; Models, Molecular; Molecular Structure; Pregnenolone; Protein Structure, Secondary; Recombinant Fusion Proteins; Substrate Specificity; Sulfotransferases; Transfection

2003