Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors.
Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors.
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DOI：
10.1016/0968-0004(90)90304-t
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发表时间：
1990-12
影响因子：
13.8
通讯作者：
Martin J. Warren;A. Scott
中科院分区：
文献类型：
--
作者：
Martin J. Warren;A. Scott
结合分子生物学和核磁共振光谱学获得的数据改变了我们对合成重要金属色素：血红素、叶绿素、维生素B12和因子F430所需生化机制演变的看法。最新的进展之一是发现了一种独特的二吡咯甲烷辅因子，它共价结合在四吡咯组装的关键酶--胆红素原脱氨酶的活性部位。我们还将讨论尿孔素环的氧化水平和发色排列，而不是它的取代模式，是如何为后来的一些酶提供必要的分子识别的，这些酶的功能是通过C-甲基化修饰模板以获得生物活性辅因子。
Data obtained using a combination of molecular biology and NMR spectroscopy has transformed our thinking about the evolution of the biochemical machinery required for the synthesis of the vital metallopigments: haem, chlorophyll, vitamin B12and factor F430. One of the most recent advances is the discovery of a unique dipyrromethane cofactor that is bound covalently at the active site of porphobilinogen deaminase, the key enzyme of tetrapyrrole assembly. We will also discuss how the oxidation level and chromophoric arrangement of the uroporphinoid ring, rather than its substitution pattern, provides the necessary molecular recognition for some of the later enzymes, whose function is to decorate the template by C-methylation on the way to the biologically active cofactors.