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PMID: 3421931 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.

The Biochemical journal ·Vol. 252 ·No. 3 ·1988-06-15 ·Pages 909-12

Hart GJ, Miller AD, Battersby AR

Abstract

Hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli uses a novel pyrromethane cofactor to bind the growing pyrrolic chain for hydroxymethylbilane biosynthesis [Hart, Miller, Leeper & Battersby (1987) J. Chem. Soc. Chem. Commun. 1762-1765]. We show that this cofactor is bound to the protein through the sulphur atom of a cysteine residue.

MeSH Terms
Ammonia-Lyases/metabolism Binding Sites Cysteine/analysis Hydroxymethylbilane Synthase/metabolism Macromolecular Substances Magnetic Resonance Spectroscopy Models, Chemical Porphobilinogen/metabolism
Chemicals
Macromolecular Substances dipyrromethane cofactor Porphobilinogen Hydroxymethylbilane Synthase Ammonia-Lyases Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hart G J
University of Cambridge Chemical Laboratory, U.K.
Miller A D
Battersby A R
References (9)
9 references, click to expand
  1. Biosynthesis of the pigments of life: formation of the macrocycle.
    Nature. 1980 May 1;285(5759):17-21 PMID: 6769048
  2. Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.
    Biochem J. 1981 Apr 1;195(1):177-81 PMID: 6975621
  3. Reassessment of Ellman's reagent.
    Methods Enzymol. 1983;91:49-60 PMID: 6855597
  4. Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.
    Biochem J. 1984 Aug 15;222(1):93-102 PMID: 6433896
  5. The biosynthesis of porphyrins, chlorophylls, and vitamin B12.
    Nat Prod Rep. 1985 Feb;2(1):19-47 PMID: 3895052
  6. The biosynthesis of porphyrins, chlorophylls, and vitamin B12.
    Nat Prod Rep. 1985 Dec;2(6):561-80 PMID: 3913886
  7. Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12.
    Nucleic Acids Res. 1986 Aug 11;14(15):6215-26 PMID: 3529035
  8. Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.
    Biochem J. 1986 Nov 15;240(1):273-6 PMID: 3548707
  9. Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase.
    FEBS Lett. 1987 Dec 10;225(1-2):87-92 PMID: 3079571
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2520909
Published
1988-06-15
Pages
909-12
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1149235
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2520909 PMC Full Text View journal details
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