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PMID: 3196304 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.

The Biochemical journal ·Vol. 254 ·No. 3 ·1988-09-15 ·Pages 915-8

Miller AD, Hart GJ, Packman LC, Battersby AR

Abstract

The pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli is bound to the protein through the sulphur atom of a cysteine residue [Hart, Miller & Battersby (1988) Biochem. J. 252, 909-912; Beifuss, Hart, Miller & Battersby (1988) Tetrahedron Lett. 29, 2591-2594]. We show that the pyrromethane-binding residue is cysteine-242.

MeSH Terms

Amino Acid Sequence Ammonia-Lyases/metabolism Cysteine/analysis Hydroxymethylbilane Synthase/metabolism Molecular Sequence Data Peptide Fragments/analysis Porphobilinogen/metabolism Protein Binding Sulfur/analysis

Chemicals

Peptide Fragments dipyrromethane cofactor Sulfur Porphobilinogen Hydroxymethylbilane Synthase Ammonia-Lyases Cysteine

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Miller A D

University of Cambridge Chemical Laboratory, U.K.

Hart G J

Packman L C

Battersby A R

References (12)

12 references, click to expand

Biosynthesis of the pigments of life: formation of the macrocycle.
Nature. 1980 May 1;285(5759):17-21 PMID: 6769048
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
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
The biosynthesis of porphyrins, chlorophylls, and vitamin B12.
Nat Prod Rep. 1985 Feb;2(1):19-47 PMID: 3895052
The biosynthesis of porphyrins, chlorophylls, and vitamin B12.
Nat Prod Rep. 1985 Dec;2(6):561-80 PMID: 3913886
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.
Biochem J. 1988 Jun 15;252(3):909-12 PMID: 3421931
Primary structure of the activation segment of procarboxypeptidase A from porcine pancreas.
Biochem Biophys Res Commun. 1986 Dec 15;141(2):517-23 PMID: 3801014
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
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
Amino acid sequence of rat mast cell protease I (chymase).
Biochemistry. 1987 Nov 3;26(22):6988-94 PMID: 3122823
The biosynthesis of porphyrins, chlorophylls, and vitamin B12.
Nat Prod Rep. 1987 Aug;4(4):441-69 PMID: 3325863
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

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2540915

Published

1988-09-15

Pages

915-8

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1135172

Subset

Grants

Wellcome Trust · United Kingdom

External Links

PubMed source DOI: 10.1042/bj2540915 PMC Full Text View journal details

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Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.

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