Nuclear magnetic resonance studies of D2O-substrate exchange reactions catalyzed by glutamic pyruvic and glutamic oxaloacetic transaminases.
作者： U. M. Babu , R. B. Johnston
DOI: 10.1021/BI00670A037
关键词: Enzyme 、 Nuclear magnetic resonance 、 Conjugated system 、 Glycine 、 Alpha (ethology) 、 GTP' 、 Chemistry 、 Catalysis 、 Substrate (chemistry) 、 Beta (finance)
摘要: Nuclear magnetic resonance studies in D2O (greater than 90%) with glutamic pyruvate transaminase (GTP) (2.6.1.2) demonstrate that this enzyme catalyzes the rapid exchange of both alpha and beta hydrogens L-alanine, only one hydrogen glycine, fluoropyruvate. When L-alanine undergo enzyme-catalyzed exchange, product may have 1, 2 or 3 exchanged. The is stimulated by addition catalytic amounts copartner transaminations reaction. A mechanism proposed for an extension conjugated system to include carbons explain labilization hydrogens.
acs.org
sci-hub.se 参考文章(15)
J. Harley-Mason, Mechanism of transaminase action Archives of Biochemistry and Biophysics. ,vol. 93, pp. 178- ,(1961) , 10.1016/0003-9861(61)90332-0
William Gibb, Jonathan Jeffery, The steric course with respect to the reduced nicotinamide-adenine dinucleotide of the reduction of 3-oxo steroids catalysed by cortisone reductase. FEBS Journal. ,vol. 34, pp. 395- 400 ,(1973) , 10.1111/J.1432-1033.1973.TB02771.X
Ulrich WALTER, Hilmar LUTHE, Hans-Dieter SOLING, Fritz GERHART, Hydrogen Exchange at the β‐Carbon of Amino Acids during Transamination FEBS Journal. ,vol. 59, pp. 395- 403 ,(1975) , 10.1111/J.1432-1033.1975.TB02467.X
U.M. Babu, R.B. Johnston, L.C. McNeff, A general NMR method for the assay of racemase activity with optically active or optically inactive substrates Analytical Biochemistry. ,vol. 63, pp. 208- 213 ,(1975) , 10.1016/0003-2697(75)90206-7
A. E. Brattnshtbin, M. M. Shemyakin, Theory of the process of amino-acid metabolism, catalysed by pyridoxal enzymes. Biokhimiya. ,vol. 18, pp. 393- 411 ,(1953)
David E. Metzler, Miyoshi Ikawa, Esmond E. Snell, A General Mechanism for Vitamin B6-catalyzed Reactions1 Journal of the American Chemical Society. ,vol. 76, pp. 648- 652 ,(1954) , 10.1021/JA01632A004
TAIRO OSHIMA, NOBUO TAMIYA, AN EXCHANGE OF β-HYDROGEN OF AMINO ACID WITH MEDIUM WATER BY TRANSAMINASE ACTION Journal of Biochemistry. ,vol. 46, pp. 1675- 1677 ,(1959) , 10.1093/OXFORDJOURNALS.JBCHEM.A126971
Mary A. Hilton, Frederick W. Barnes, Sarah S. Henry, Theodore Enns, Mechanisms in enzymatic transamination; rate of exchange of the hydrogen of aspartate. Journal of Biological Chemistry. ,vol. 209, pp. 743- 754 ,(1954) , 10.1016/S0021-9258(18)65502-4
Mary A. Hilton, Frederick W. Barnes, Theodore Enns, MECHANISMS IN ENZYMATIC TRANSAMINATION: EFFECT OF α-KETOGLUTARATE CONCENTRATION ON THE RATE OF EXCHANGE OF THE HYDROGEN OF ASPARTATE Journal of Biological Chemistry. ,vol. 219, pp. 833- 843 ,(1956) , 10.1016/S0021-9258(18)65741-2
A J Cooper, Proton magnetic resonance studies of glutamate-alanine transaminase-catalyzed deuterium exchange. Evidence for proton conservation during prototropic transfer from the alpha carbon of L-alanine to the C4-position of pyridoxal 5'-phosphate. Journal of Biological Chemistry. ,vol. 251, pp. 1088- 1096 ,(1976) , 10.1016/S0021-9258(17)33805-X