Biochemical and Biophysical Research Communications
Volume 155, Issue 1, 30 August 1988, Pages 317-323
A single amino acid substitution converts cytochrome P45014DM to an inactive form, cytochrome P450SG1: Complete primary structures deduced from cloned DNAs
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Evaluation of structural features in fungal cytochromes P450 predicted to rule catalytic diversification
2013, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :Finally, replacement of threonine with alanine at position 315 reduced catalytic efficiency (Vmax/Km) to 27% that of the control [64]. Interestingly, a catalytically inactive CYP51F1 variant from Saccharomyces cerevisiae was recognized to bear a G310D mutation obviously associated with active-site distortion [66]. Hence, G310, mapping with G303 in the Candida albicans enzyme was deemed a determinant in maintaining integrity of the heme environment to afford proper orientation of sterols toward the iron-oxene entity [60].
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Copyright © 1988 Published by Elsevier Inc.