Interaction of Pyridine Nucleotide Substrates with Escherichia coli Dihydrodipicolinate Reductase: Thermodynamic and Structural Analysis of Binary Complexes

E. coli dihydrodipicolinate reductase exhibits unusual nucleotide specificity, with NADH being kinetically twice as effective as NADPH as a reductant as evidenced by their relative V/K values. To investigate the nature of the interactions which determine this specificity, we performed isothermal tit...

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Veröffentlicht in:	Biochemistry (Easton) 1996-10, Vol.35 (41), p.13294-13302
Hauptverfasser:	Reddy, Sreelatha G, Scapin, Giovanna, Blanchard, John S
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Crystallography, X-Ray Dihydrodipicolinate Reductase Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Kinetics Models, Chemical Molecular Structure NAD - metabolism NADP - metabolism Nucleotides - chemistry Nucleotides - metabolism Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - metabolism Oxidoreductases Acting on CH-CH Group Donors Phosphorylation Protein Conformation Substrate Specificity Thermodynamics
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