The CYP79A1 catalyzed conversion of tyrosine to (E)-p-hydroxyphenylacetaldoxime unravelled using an improved method for homology modeling

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• 作者：Dario Vazquez-Albacete^a ; ¹ ; Marco Montefiori^b ; ¹ ; Stefan Kol^a ; Mohammed Saddik Motawia^c ; ^d ; Birger Lindberg Mø ; ller^c ; ^d ; Lars Olsen^b ; Morten H.H. Nø ; rholm^a ; ^d ; ^{morno@biosustain.dtu.dk}
• 关键词：Cytochrome P450 ; Cyanogenic glucosides ; Enzymes ; Homology modeling ; Docking ; Membrane proteins
• 刊名：Phytochemistry
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：135
• 期：Complete
• 页码：8-17
• 全文大小：2222 K
• 卷排序：135

文摘

A modified hybrid structure strategy is used to model the Sorghum bicolor CYP79A1. The model provides detailed insights into the mechanism of cyanogenic glycoside biosynthesis. Docking of substrate in the model reveal interactions with R152, D347 and T534. Site directed mutagenesis confirm interactions of the key amino acid residues. Conservation of R152 and D347 is observed in other tyrosine-catalyzing CYP79 enzymes.