Chopping and Changing: the Evolution of the Flavin-dependent Monooxygenases
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- 作者：Maria Laura Mascotti1 ; mlmascotti@unsl.edu.ar" class="auth_mail" title="E-mail the corresponding author ; Maximiliano Juri Ayub1 ; Nicholas Furnham2 ; Janet M. Thornton3 ; Roman A. Laskowski3 ; roman@ebi.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：FAD ; flavin adenine dinucleotide ; FMN ; flavin mononucleotide ; FMO ; flavin monooxygenase ; MDA ; multidomain architecture ; EC ; Enzyme Commission ; GR ; glutathione reductase ; PDB ; protein data bank ; ML ; maximum likelihood ; BS ; bootstrap ; BVMO ; Baeyer&ndash ; Villiger monooxygenase ; NMO ; N-hydroxylating monooxygenases ; MAO ; monoamine oxidase ; PHBH ; p-hydroxybenzoate hydroxylase ; MSA ; multiple sequence alignment
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3131-3146
- 全文大小：1932 K
文摘
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Changes in domain architectures reflect the phylogeny of flavin monooxygenases.
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Recruitment of different domains has been the main force driving its evolution.
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A notable feature of flavin monooxygenases is that the flavin adenine dinucleotide-binding domain is split.
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Classes of monooxygenases emerged from an ancestral domain by structural changes.