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| TETRAPYRROLE ASSEMBLY AND MODIFICATION INTO THE LIGANDS OF BIOLOGICALLY FUNCTIONAL COFACTORS |
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| Author(s): WARREN MJ, SCOTT AI |
| Source: TRENDS IN BIOCHEMICAL SCIENCES Volume: 15 Issue: 12 Pages: 486-491 Published: DEC 1990 |
| Times Cited: 67 References: 30 |
| Abstract: 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. |
| Document Type: Review |
| Language: English |
| Reprint Address: WARREN, MJ (reprint author), TEXAS A&M UNIV SYST, CTR BIOL NUCL MAGNET RESONANCE, DEPT CHEM, COLLEGE STN, TX 77843 USA |
| Publisher: ELSEVIER SCI LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, OXON, ENGLAND OX5 1GB |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: EP182 |
| ISSN: 0968-0004 |
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