Biochemistry. How active sites communicate in thiamine enzymes.
Jordan
Frank
F
Department of Chemistry, Rutgers University, Newark, NJ 07102, USA. frjordan@newark.rutgers.edu
D019943:Amino Acid Substitution; D001665:Binding Sites; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D019281:Dimerization; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D018698:Glutamic Acid / Q000737:chemistry; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons; D030481:Pyruvate Dehydrogenase (Lipoamide) / Q000737:chemistry* / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism*
D021122:Protein Subunits; D011522:Protons; D011768:Pyruvate Dehydrogenase Complex; D018698:Glutamic Acid; D030481:Pyruvate Dehydrogenase (Lipoamide); D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D013835:Thiamine Pyrophosphate