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Updated: Feb 20, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
Drew R Tietz1, Allison M Colthart2, Susan Sondej Pochapsky1
1Department of Chemistry, Brandeis University, MS 015, 415 South St, Waltham, MA, 02453, USA.
Abstract:
Cytochrome P450 monooxygenases CYP101A1 and MycG catalyze regio- and stereospecific oxidations of their respective substrates, d-camphor and mycinamicin IV. Despite the low sequence homology between the two enzymes (29% identity) and differences in size and hydrophobicity of their substrates, the conformational changes that occur upon substrate binding in both enzymes as determined by solution NMR methods show some striking similarities. Many of the same secondary structural features in both enzymes are perturbed, suggesting the existence of a common mechanism for substrate binding and recognition in the P450 superfamily.
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