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The kinetic and spectral characterization of the E. coli-expressed mammalian CYP4A7: cytochrome b5 effects vary with substrate.
Saturation kinetics studies performed with heme-depleted cytochrome b5 yielded turnover numbers of 118 and 74 min(-1) and Km values of 74 and 25 microM with laurate and myristate, respectively, indicating that cyto chrome b5 is not involved in electron transfer but rather plays a conformational role. Expand
Expressed CYP4A4 metabolism of prostaglandin E(1) and arachidonic acid.
The enzyme was purified, and its activity with substrates prostaglandin E(1) (PGE(1)) and AA was examined, and a conformational change occurred in CYP4A4 protein upon binding of cyt b(5) or apo b( 5). Expand
Identification of unique amino acids that modulate CYP4A7 activity.
Experimental results provide insight regarding the residues responsible for modulation of substrate specificity, affinity, and kinetics, as well as possible localization within the enzyme structure based on comparisons with homologous, known cytochrome P450 structures. Expand