翻訳と辞書 Words near each other ・ 4-Hydroxycinnamate decarboxylase ・ 4-Hydroxycoumarin synthase ・ 4-Hydroxycoumarins ・ 4-Hydroxycyclohexanecarboxylate dehydrogenase ・ 4-Hydroxycyclophosphamide ・ 4-hydroxyglutamate transaminase ・ 4-hydroxymandelate oxidase ・ 4-hydroxymandelate synthase ・ 4-Hydroxymandelic acid ・ 4-hydroxymuconic-semialdehyde dehydrogenase ・ 4-Hydroxynonenal ・ 4-hydroxynonenal-lysine ・ 4-hydroxyphenylacetaldehyde dehydrogenase ・ 4-hydroxyphenylacetaldehyde oxime monooxygenase ・ 4-hydroxyphenylacetate 1-monooxygenase ・ 4-Hydroxyphenylacetate 3-monooxygenase ・ 4-hydroxyphenylacetate decarboxylase ・ 4-Hydroxyphenylacetic acid ・ 4-Hydroxyphenylacetone ・ 4-hydroxyphenylpyruvate decarboxylase ・ 4-Hydroxyphenylpyruvate dioxygenase ・ 4-hydroxyphenylpyruvate dioxygenase inhibitor ・ 4-hydroxyphenylpyruvate oxidase ・ 4-Hydroxyphenylpyruvic acid ・ 4-hydroxyproline epimerase ・ 4-hydroxyquinoline 3-monooxygenase ・ 4-Hydroxytestosterone ・ 4-hydroxythreonine-4-phosphate dehydrogenase ・ 4-Iodo-N,N-dimethylaniline ・ 4-Iodopropofol Dictionary Lists mini英和辞書 mini和英辞書 Webster 1913 Latin-English FOLDOC Wikipedia English ウィキペディア

翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク 4-Hydroxyphenylacetate 3-monooxygenase ： ウィキペディア英語版 4-Hydroxyphenylacetate 3-monooxygenase 4-hydroxyphenylacetate 3-monooxygenase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylacetate + FADH2 + O2 $\backslash rightleftharpoons$ 3,4-dihydroxyphenylacetate + FAD + H2O This reaction is the first step in a pathway found in enteric bacteria such as Escherichia coli and soil bacteria such as Pseudomonas putida which degrades 4-hydroxyphenylacetate (4-HPA), allowing these bacteria to use 4-HPA and other aromatic compounds found in mammalian digestive tracts or in soil as a carbon source. While most known flavin monooxygenases use NADH or NADPH as substrates (and use the flavins FAD or FMN as prosthetic groups ), this enzyme is part of a two-component system, in which a flavin oxidoreductase partner () regenerates FADH2 by oxidizing NADH to NAD+. hpaB and hpaC, the 4-HPA oxygenase and reductase partner proteins (respectively) of ''E. coli'' strain W, were the first two-component flavin monoxygenase system identified. While known examples of this enzyme share a common catalytic mechanism and likely evolutionary origin, they differ with respect to regulation and ability to substitute FMNH2 for FADH2 as a substrate. ==Structure== This enzyme is a tetramer which forms as a dimer of dimers. Sequence alignments of the Thermus thermophilus and ''E. coli'' hpaB enzymes show structural similarity to each other and to the oxygenase components of other bacterial two-component monooxygenases for compounds such as phenol and chlorophenol.〔 Each monomer of this protein consists of an N-terminal alpha-helical domain, a middle beta barrel domain, and a C-terminal "tail" helix. FADH2 is bound by a groove between these domains; this binding event causes a loop in the middle domain to change position, preforming a binding site for 4-HPA. At this point, multiple residues act to stabilize catalytic intermediates by hydrogen-bonding to the peroxide bound to FAD, as well as to the hydroxyl group of 4-HPA's phenol moiety (stabilizing its dienone transition state - see Mechanism). The loop which moves to form the 4-HPA binding site when FADH2 binds provides catalytic specificity by hydrogen-bonding to 4-HPA's carboxylic acid moiety.〔 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「4-Hydroxyphenylacetate 3-monooxygenase」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.