The tryptophanase from Escherichia coli K-12. II. Comparison of the thermal stabilities of apo-, holo-, and hybrid enzymes.
D001059:Apoproteins; D001665:Binding Sites; D001894:Borohydrides; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D006836:Hydro-Lyases; D007700:Kinetics; D046911:Macromolecular Substances; D010084:Oxidation-Reduction; D011732:Pyridoxal Phosphate; D012964:Sodium; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D013997:Time Factors; D014368:Tryptophanase / Q000302:isolation & purification; D014508:Urea
D001059:Apoproteins; D001894:Borohydrides; D046911:Macromolecular Substances; D011732:Pyridoxal Phosphate; D014508:Urea; D012964:Sodium; D014368:Tryptophanase; D006836:Hydro-Lyases