Publications

• Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme.

  Shoolingin-Jordan P.M., Warren M.J., Awan S.J.

  The assembly process of the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase holoenzyme is initiated by the reaction of the porphobilinogen deaminase apoenzyme with preuroporphyrinogen. The resulting enzyme-bound tetrapyrrole (bilane) is equivalent to the holoenzyme intermedia ... >> More

  The assembly process of the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase holoenzyme is initiated by the reaction of the porphobilinogen deaminase apoenzyme with preuroporphyrinogen. The resulting enzyme-bound tetrapyrrole (bilane) is equivalent to the holoenzyme intermediate complex ES2 and yields the dipyrromethane cofactor by reactions of the normal catalytic cycle. These observations indicate that preuroporphyrinogen, rather than porphobilinogen, is the preferred precursor for the dipyrromethane cofactor and explain the existence of the D84A and D84N deaminase mutants as catalytically inactive ES2 complexes. << Less

  Biochem J 316:373-376(1996) [PubMed] [EuropePMC]

• Tetrapyrroles: the pigments of life.

  Battersby A.R.

  Nat Prod Rep 17:507-526(2000) [PubMed] [EuropePMC]

• Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site.

  Louie G.V., Brownlie P.D., Labert R., Cooper J.B., Blundell T.L., Wood S.P., Warren M.J., Woodcock S.C., Jordan P.M.

  The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is cov ... >> More

  The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins. The X-ray structure and results from site-directed mutagenesis provide evidence for a single catalytic site. Interdomain flexibility may aid elongation of the polypyrrole product in the active-site cleft of the enzyme. << Less

  Nature 359:33-39(1992) [PubMed] [EuropePMC]

• Studies on porphobilinogen deaminase and uroporphyrinogen 3 cosynthase from human erythrocytes.

  Frydman R.B., Feinstein G.

  Biochim Biophys Acta 350:358-373(1974) [PubMed] [EuropePMC]

• Biosynthesis of the pigments of life: formation of the macrocycle.

  Battersby A.R., Fookes C.J., Matcham G.W., McDonald E.

  The organic nuclei of chlorophylls, haems, cytochromes and vitamin B12 are biosynthesised from a single tetrapyrrolic intermediate which has an unexpected, rearranged structure. The mechanism of biosynthesis of this key intermediate has now been characterised in detail. Some of the information the ... >> More

  The organic nuclei of chlorophylls, haems, cytochromes and vitamin B12 are biosynthesised from a single tetrapyrrolic intermediate which has an unexpected, rearranged structure. The mechanism of biosynthesis of this key intermediate has now been characterised in detail. Some of the information thereby obtained is also of use in the investigation of human diseases such as the porphyrias. << Less

  Nature 285:17-21(1980) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Evidence for participation of aspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene from Escherichia coli.

  Woodcock S.C., Jordan P.M.

  The role of aspartate-84, an invariant residue in the active site cleft of Escherichia coli porphobilinogen deaminase, has been investigated by site-directed mutagenesis. Substitution of aspartate-84 by glutamate results in an enzyme that retains less than 1% of its activity and which can form hig ... >> More

  The role of aspartate-84, an invariant residue in the active site cleft of Escherichia coli porphobilinogen deaminase, has been investigated by site-directed mutagenesis. Substitution of aspartate-84 by glutamate results in an enzyme that retains less than 1% of its activity and which can form highly stable enzyme-intermediate complexes. Substitution of aspartate-84 by either alanine or asparagine, however, results in proteins unable to catalyze the formation of preuroporphyrinogen but which, nevertheless, appear able to assemble the dipyrromethane cofactor. The mechanisms of the tetramerization reaction and cofactor assembly are discussed. << Less

  Biochemistry 33:2688-2695(1994) [PubMed] [EuropePMC]