Compounds > 7,8-diaminopelargonic acid

7,8-diaminopelargonic acid and s-adenosylmethionine

7,8-diaminopelargonic acid has been researched along with s-adenosylmethionine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's4 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Eliot, AC; Kirsch, JF; Sandmark, J; Schneider, G1
Eliot, AC; Famm, K; Kirsch, JF; Sandmark, J; Schneider, G1
Atta, M; Fontecave, M; Mulliez, E1
Chatterjee, NP; Howitt, CL; Luan, L; Perkins, JB; Pero, JG; Van Arsdell, SW; Yocum, RR1

Reviews

1 review(s) available for 7,8-diaminopelargonic acid and s-adenosylmethionine

ArticleYear
S-adenosylmethionine: nothing goes to waste.
    Trends in biochemical sciences, 2004, Volume: 29, Issue:5

    Topics: 4-Butyrolactone; Acetyltransferases; Amino Acids, Cyclic; Amino Acids, Diamino; Animals; Cyclopropanes; Fatty Acids; Humans; Intramolecular Transferases; Models, Chemical; Nucleoside Q; Ribonucleotide Reductases; S-Adenosylmethionine; Spermidine; Uridine

2004

Other Studies

3 other study(ies) available for 7,8-diaminopelargonic acid and s-adenosylmethionine

ArticleYear
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation.
    Biochemistry, 2002, Oct-22, Volume: 41, Issue:42

    Topics: Alanine; Amino Acids, Diamino; Arginine; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli Proteins; Hydrogen-Ion Concentration; Imines; Kinetics; Mutagenesis, Site-Directed; S-Adenosylmethionine; Spectrophotometry; Stereoisomerism; Substrate Specificity; Transaminases

2002
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.
    Biochemistry, 2004, Feb-10, Volume: 43, Issue:5

    Topics: Alanine; Amination; Amino Acids, Diamino; Arginine; Binding Sites; Catalysis; Conserved Sequence; Crystallography, X-Ray; Escherichia coli Proteins; Glutamine; Kinetics; Lysine; Mutagenesis, Site-Directed; S-Adenosylmethionine; Substrate Specificity; Transaminases; Tyrosine

2004
Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction.
    Biotechnology and bioengineering, 2005, Jul-05, Volume: 91, Issue:1

    Topics: Amino Acids; Amino Acids, Diamino; Bacillus subtilis; Bacterial Proteins; Biotin; Gene Expression Regulation, Bacterial; Lysine; Protein Engineering; Recombinant Proteins; S-Adenosylmethionine; Signal Transduction; Transaminases

2005