Warren, M.J. and Scott, A.I. (1990) Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors. Trends in Biochemical Sciences, 15 (12). pp. 486-91. ISSN 0968-0004 .
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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 B12 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 porphobillinogen 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.
|Additional information:||Review journal article|
|Uncontrolled keywords:||Binding Sites Hydroxymethylbilane Synthase/chemistry Ligands Methylation Porphobilinogen/chemistry Pyrroles/*chemistry Tetrapyrroles Uroporphyrinogens/*chemistry/metabolism|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Martin Warren|
|Date Deposited:||03 Oct 2009 12:02|
|Last Modified:||14 Jan 2010 14:42|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/11122 (The current URI for this page, for reference purposes)|
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