Substrate recognition by two different P450s: Evidence for conserved roles in a common fold

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 co...

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Autores principales: Tietz, Drew R., Colthart, Allison M., Sondej Pochapsky, Susan, Pochapsky, Thomas C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5648816/
https://www.ncbi.nlm.nih.gov/pubmed/29051575
http://dx.doi.org/10.1038/s41598-017-14011-w
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author Tietz, Drew R.
Colthart, Allison M.
Sondej Pochapsky, Susan
Pochapsky, Thomas C.
author_facet Tietz, Drew R.
Colthart, Allison M.
Sondej Pochapsky, Susan
Pochapsky, Thomas C.
author_sort Tietz, Drew R.
collection PubMed
description 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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spelling pubmed-56488162017-10-26 Substrate recognition by two different P450s: Evidence for conserved roles in a common fold Tietz, Drew R. Colthart, Allison M. Sondej Pochapsky, Susan Pochapsky, Thomas C. Sci Rep Article 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. Nature Publishing Group UK 2017-10-19 /pmc/articles/PMC5648816/ /pubmed/29051575 http://dx.doi.org/10.1038/s41598-017-14011-w Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Tietz, Drew R.
Colthart, Allison M.
Sondej Pochapsky, Susan
Pochapsky, Thomas C.
Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title_full Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title_fullStr Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title_full_unstemmed Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title_short Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
title_sort substrate recognition by two different p450s: evidence for conserved roles in a common fold
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5648816/
https://www.ncbi.nlm.nih.gov/pubmed/29051575
http://dx.doi.org/10.1038/s41598-017-14011-w
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