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How Are Substrate Binding and Catalysis Affected by Mutating Glu(127) and Arg(161) in Prolyl-4-hydroxylase? A QM/MM and MD Study
Prolyl-4-hydroxylase is a vital enzyme for human physiology involved in the biosynthesis of 4-hydroxyproline, an essential component for collagen formation. The enzyme performs a unique stereo- and regioselective hydroxylation at the C(4) position of proline despite the fact that the C(5) hydrogen a...
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| Vydáno v: | Front Chem |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Frontiers Media S.A.
2017
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5684110/ https://ncbi.nlm.nih.gov/pubmed/29170737 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3389/fchem.2017.00094 |
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