Site-directed mutagenesis of glyceraldehyde-3-phosphate dehydrogenase reveals the role of residue Ser148
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/2/7/559/4377235/2-7-559.pdf
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Thermal Unfolding Used As a Probe To Characterize the Intra- and Intersubunit Stabilizing Interactions in Phosphorylating d-Glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus;Biochemistry;2002-05-18
2. Comparison of the Structures of Wild-type and a N313T Mutant ofEscherichia coliGlyceraldehyde 3-Phosphate Dehydrogenases: Implication for NAD Binding and Cooperativity;Journal of Molecular Biology;1996-04
3. Characterization of the two anion-recognition sites of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis and chemical modification;Biochemistry;1994-03-22
4. Inhibition of glyceraldehyde-3-phosphate dehydrogenase by phosphorylated epoxides and .alpha.-Enones;Biochemistry;1994-01-11
5. Inhibition of the glycolytic enzymes in the trypanosome: An approach in the development of new leads in the therapy of parasitic diseases;Pharmacology & Therapeutics;1993-01
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