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Chemistry & Biology|August 1, 1995
Biosynthesis of porphyrins and related macrocycles, Part 43. Isolation and characterization of intermediates of coenzyme B12 biosynthesis, a cobyrinic acid triamide, the a,c-diamide and their Co-(5'-deoxy-5'-adenosyl) derivatives, from Propionibacterium shermaniiF Kiuchi, F J Leeper, A R Battersby
European Journal of Biochemistry|July 1, 1995
Expression, purification and characterisation of the product from the Bacillus subtilis hemD gene, uroporphyrinogen III synthaseN P Stamford, A Capretta, A R Battersby
The Biochemical Journal|November 15, 1986
Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coliG J Hart, C Abell, A R Battersby
The Biochemical Journal|August 15, 1984
Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residueG J Hart, F J Leeper, A R Battersby
The Biochemical Journal|June 15, 1988
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residueG J Hart, A D Miller, A R Battersby
The Biochemical Journal|January 1, 1981
Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kineticsD C Williams, G S Morgan, E McDonald, et al.
Nature|May 1, 1980
Biosynthesis of the pigments of life: formation of the macrocycleA R Battersby, C J Fookes, G W Matcham, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1990
Biosynthesis of vitamin B12: structure of precorrin-6x octamethyl esterD Thibaut, F Blanche, L Debussche, et al.
The Biochemical Journal|September 15, 1988
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242A D Miller, G J Hart, L C Packman, et al.
The Biochemical Journal|October 15, 1990
Investigation of putative active-site lysine residues in hydroxymethylbilane synthase. Preparation and characterization of mutants in which (a) Lys-55, (b) Lys-59 and (c) both Lys-55 and Lys-59 have been replaced by glutamineA Hädener, P R Alefounder, G J Hart, et al.
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