Availability of porphobilinogen controls appearance of porphobilinogen deaminase activity in Escherichia coli K-12.

A hemin-permeable hemB mutant had no 5-aminolevulinate dehydratase (ALA D) and extremely low porphobilinogen deaminase (PBG D) activity. When the structural gene for hemB was introduced into this strain on a single-copy plasmid, both activities were observed. When the mutant was grown on PBG, normal...

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Pubblicato in:	J Bacteriol
Autori principali:	Umanoff, H, Russell, C S, Cosloy, S D
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	American Society for Microbiology (ASM) 1988
Soggetti:	Research Article
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC211550/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3049558/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.170.10.4969-4971.1988
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