The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH-Reference-Cited by-同舟云学术

The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH

Published:2011-09 Issue:2 Volume:513 Page:71-80
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Bobyk Kostyantyn D.,Kim Sang Gon,Kumar Vidya Prasanna,Kim Sung-Kun,West Ann H.,Cook Paul F.

Funder

National Institutes of Health

Grayce B. Kerr Endowment to the University of Oklahoma

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. D.B. Northrop, 1977. in: W.W. Cleland, M.H. O’Leary, D.B. Northrop (Eds.), In Isotope Effects on Enzyme-Catalyzed Reactions, University Park Press, Baltimore MD, pp 122–152.

2. Mechanistic deductions from isotope effects in multireactant enzyme mechanisms

3. Lysine biosynthesis in selected pathogenic fungi: characterization of lysine auxotrophs and the cloned LYS1 gene of Candida albicans

4. Lysine biosynthesis and metabolism in fungi

5. Structural Studies of the Final Enzyme in the α-Aminoadipate Pathway-Saccharopine Dehydrogenase from Saccharomyces cerevisiae

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1. Supporting role of lysine 13 and glutamate 16 in the acid–base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae;Archives of Biochemistry and Biophysics;2012-06

2. Evidence in Support of Lysine 77 and Histidine 96 as Acid–Base Catalytic Residues in Saccharopine Dehydrogenase from Saccharomyces cerevisiae;Biochemistry;2012-01-23