Page last updated: 2024-09-03

adenylosuccinate and asparagine

adenylosuccinate has been researched along with asparagine in 2 studies

Compound Research Comparison

Studies (adenylosuccinate)	Trials (adenylosuccinate)	Recent Studies (post-2010) (adenylosuccinate)	Studies (asparagine)	Trials (asparagine)	Recent Studies (post-2010) (asparagine)
52	1	5	6,819	41	1,398

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
Colman, RF; Palenchar, JB	1
Colman, RF; Segall, ML	1

Other Studies

2 other study(ies) available for adenylosuccinate and asparagine

Article	Year
Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role. Biochemistry, 2003, Feb-25, Volume: 42, Issue:7 Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Aminoimidazole Carboxamide; Arginine; Asparagine; Bacillus subtilis; Bacterial Proteins; Circular Dichroism; Enzyme Activation; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Threonine	2003
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis. Biochemistry, 2004, Jun-15, Volume: 43, Issue:23 Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Animals; Arginine; Asparagine; Bacillus subtilis; Binding Sites; Catalysis; Circular Dichroism; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Sequence Alignment; Thermodynamics	2004

Article

Year

Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role.

Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Aminoimidazole Carboxamide; Arginine; Asparagine; Bacillus subtilis; Bacterial Proteins; Circular Dichroism; Enzyme Activation; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Threonine

2003

Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.

Biochemistry, 2004, Jun-15, Volume: 43, Issue:23

Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Animals; Arginine; Asparagine; Bacillus subtilis; Binding Sites; Catalysis; Circular Dichroism; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Sequence Alignment; Thermodynamics

2004