TETRAPYRROLE ASSEMBLY AND MODIFICATION INTO THE LIGANDS OF BIOLOGICALLY FUNCTIONAL COFACTORS

被引:99
作者
WARREN, MJ
SCOTT, AI
机构
[1] Center for Biological NMR, Department of Chemistry, Texas A and M University, College Station
关键词
D O I
10.1016/0968-0004(90)90304-T
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 B-12 and 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.
引用
收藏
页码:486 / 491
页数:6
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