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PMID: 2510713 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).

The Biochemical journal ·Vol. 262 ·No. 1 ·1989-08-15 ·Pages 119-24

Miller AD, Packman LC, Hart GJ, Alefounder PR, Abell C, Battersby AR

Abstract

A recombinant strain of Escherichia coli has been constructed that produces approx. 200 times the amount of hydroxymethylbilane synthase found in wild-type E. coli [Hart, Abell & Battersby (1986) Biochem. J. 240, 273-276]. Enzyme purified from this strain is shown to be permanently inactivated by pyridoxal 5'-phosphate/NaB1H3(3)H1. The inactivation is not complete despite the fact that approx. 1 mol of lysine residues is modified per mol of enzyme. Evidence is gained showing that (a) modification of one of two conserved lysine residues (Lys-55 or Lys-59) results in inactivation of hydroxymethylbilane synthase and (b) these lysine residues are present in or close to the active site.

MeSH Terms
Amino Acid Sequence Ammonia-Lyases/antagonists & inhibitors Binding Sites Escherichia coli/enzymology Hydroxymethylbilane Synthase/antagonists & inhibitors Lysine/metabolism Plasmids Protease Inhibitors/metabolism Pyridoxal Phosphate/pharmacology
Chemicals
Protease Inhibitors Pyridoxal Phosphate Hydroxymethylbilane Synthase Ammonia-Lyases Lysine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Miller A D
University Chemical Laboratory, Cambridge, U.K.
Packman L C
Hart G J
Alefounder P R
Abell C
Battersby A R
References (19)
19 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2620119
Published
1989-08-15
Pages
119-24
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1133237
Subset
IM
Grants
Wellcome Trust · United Kingdom
External Links
PubMed source DOI: 10.1042/bj2620119 PMC Full Text View journal details
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