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引用本文的文献
1
Utilization of the free energy of the reversible binding of protein and modifying agent towards the rate-enhancement of protein covalent modification.
Biochem J. 1990 Aug 1;269(3):835-8. doi: 10.1042/bj2690835.
本文引用的文献
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Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetase.
Arch Biochem Biophys. 1980 Apr 15;201(1):313-21. doi: 10.1016/0003-9861(80)90516-0.
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The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming).
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Kinetics of protein modification reactions.
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Kinetic analysis of protein modification reactions at equilibrium.
Biochem J. 1989 Nov 1;263(3):855-9. doi: 10.1042/bj2630855.
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The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.
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Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase.
Biochemistry. 1979 Dec 25;18(26):5909-17. doi: 10.1021/bi00593a023.
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The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.
Biochem J. 1979 Sep 1;181(3):775-8. doi: 10.1042/bj1810775.
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Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
Biochem J. 1975 Sep;149(3):627-35. doi: 10.1042/bj1490627.
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Role of tyrosyl and arginyl residues in rat liver microsomal stearylcoenzyme A desaturase.
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Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5'-phosphate.
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