D-Glyceraldehyde-3-Phosphate Dehydrogenase Amino-Acid Sequence of the Enzyme from the Extreme Thermophile Thermus aquaticus
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb04752.x/fullpdf
Reference14 articles.
1. Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase
2. Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus
3. Purification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase fromThermus aquaticus
4. Heat Stability of a Tetrameric Enzyme, D-Glyceraldehyde-3-PhosphateDehydrogenase
5. D-Glyceraldehyde-3-Phosphate Dehydrogenase. Complete Amino-Acid Sequence of the Enzyme from Bacillus stearothermophilus
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1. Structural basis for the thermal stability of glyceraldehyde-3-phosphate dehydrogenases;International Journal of Peptide and Protein Research;2009-01-12
2. Affinity Labeling of Glyceraldehyde-3-phosphate Dehydrogenase from Sturgeon and Bacillus stearothermophilus by 3-Chloroacetylpyridine-adenine Dinucleotide;European Journal of Biochemistry;2005-03-03
3. Enthalpic and entropic consequences of the removal of disulfide bridges in ribonuclease A;Thermochimica Acta;2000-12
4. Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity;FEBS Letters;1998-11-20
5. A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii;Infection and Immunity;1996-01
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