Warren, M.J. and Bolt, E. and Woodcock, S.C. (1994) 5-Aminolevulinic Acid Synthase and Uroporphyrinogen Methylase - 2 Key Control Enzymes of Tetrapyrrole Biosynthesis and Modification. In: Symposium on the Biosynthesis of the Tetrapyrrole Pigments, held in honour of Sir Alan Battersby, March 30-April 01, 1993, CIBA FDN, LONDON, ENGLAND .
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Two enzymes which play an important role in regulation and flux control through the tetapyrrole biosynthetic pathway are considered. The Rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes are discussed and the progress being made on their recombinant expression and isolation is reported. The Escherichia coli uroporphyrinogen methylase, which is encoded by the cysG gene, is also examined. In this case evidence is provided which demonstrates that the gene product is responsible for the complete synthesis of sirohaem from uroporphyrinogen III. The enzyme is thus capable of performing two S-adenosylmethionine-dependent methylation reactions, an NADP(+)-dependent dehydrogenation and iron chelation. The uroporphyrinogen methylase is thus a small multifunctional enzyme.
|Item Type:||Conference or workshop item (Paper)|
|Uncontrolled keywords:||adenosyl-l-methionine adenosylmethionine-dependent methyltransferases 5-aminolevulinate synthase nucleotide-sequence rhodobacter-sphaeroides iii methyltransferase escherichia-coli saccharomyces-cerevisiae enzymatic-synthesis cobyrinic acid|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Martin Warren|
|Date Deposited:||21 Oct 2009 08:13|
|Last Modified:||14 Jan 2010 14:42|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/11109 (The current URI for this page, for reference purposes)|
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