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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Biopterin-dependent aromatic amino acid hydroxylase ： ウィキペディア英語版 Biopterin-dependent aromatic amino acid hydroxylase In molecular biology, the biopterin-dependent aromatic amino acid hydroxylases (abbreviated AAAH) constitute a family of aromatic amino acid hydroxylases, including phenylalanine 4-hydroxylase (), tyrosine 3-hydroxylase (), and tryptophan 5-hydroxylase (). These enzymes primarily hydroxylate phenylalanine, tyrosine, and tryptophan, respectively. These enzymes are all rate-limiting catalysts for important metabolic pathways. The proteins are structurally and functionally related, each containing iron, and catalysing ring hydroxylation of aromatic amino acids, using tetrahydrobiopterin (BH4) as a substrate. All are regulated by phosphorylation at serines in their N-termini. It has been suggested that the proteins each contain a conserved C-terminal catalytic (C) domain and an unrelated N-terminal regulatory (R) domain. It is possible that the R domains arose from genes that were recruited from different sources to combine with the common gene for the catalytic core. Thus, by combining with the same C domain, the proteins acquired the unique regulatory properties of the separate R domains. In humans, phenylalanine hydroxylase deficiency can cause of phenylketonuria, the most common inborn error of amino acid metabolism, Tryptophan hydroxylase catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of tryptophan to 5-hydroxy-L-tryptophan and tyrosine hydroxylase catalyzes the rate limiting step in catecholamine biosynthesis: the conversion of tyrosine to L-DOPA. ==References== 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「Biopterin-dependent aromatic amino acid hydroxylase」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.