Silverman et al., 1981 - Google Patents
Substituted 4-aminobutanoic acids. Substrates for gamma-aminobutyric acid alpha-ketoglutaric acid aminotransferase.Silverman et al., 1981
View PDF- Document ID
- 13664228303257273977
- Author
- Silverman R
- Levy M
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
Substituted 4-aminobutanoic acids were studied as potential irreversible inactivators of purified pig brain gamma-aminobutyric acid aminotransferase, the enzyme responsible for the degradation of the inhibitory neurotransmitter, gamma-aminobutyric acid. It was found …
- BTCSSZJGUNDROE-UHFFFAOYSA-N GABA 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E7c3Ryb2tlOm5vbmU7Zm9udC1mYW1pbHk6c2Fucy1zZXJpZjt0ZXh0LWFuY2hvcjpzdGFydDtmaWxsOiNFODQyMzUnID5PPC90ZXh0Pgo8L3N2Zz4K 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QyMzUnID5PPC90ZXh0Pgo8L3N2Zz4K NCCCC(O)=O 0 title abstract description 44
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| Ayling et al. | Kinetics of phenylalamine hydroxylase with analogs of tetrahydrobiopterin | |
| Kanamori et al. | Effect of the nitrogen source on glutamine and alanine biosynthesis in Neurospora crassa. An in vivo 15N nuclear magnetic resonance study. | |
| Kishore | Mechanism-based inactivation of bacterial kynureninase by beta-substituted amino acids. | |
| Samejima et al. | Action of decarboxylated S-adenosylmethionine analogs in the spermidine-synthesizing system from rat prostate | |
| Klinman et al. | Mechanism of the aconitate isomerase reaction | |
| Morino et al. | Evidence for the presence of a distinct subsite for binding the distal carboxyl group of dicarboxylate substrates and its role in the catalytic activity of aspartate aminotransferase | |
| Palekar et al. | Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine | |
| Allison et al. | Steady state and equilibrium exchange kinetic studies of the sheep brain glutamine synthetase reaction. | |
| Bailey et al. | Role of C6 chirality of tetrahydropterin cofactor in catalysis and regulation of tyrosine and phenylalanine hydroxylases | |
| Srinivasan et al. | Reversible reduction of an. alpha.-imino acid to an. alpha.-amino acid catalyzed by glutamate dehydrogenase: effect of ionizable functional groups |