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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1988
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC211550/ https://ncbi.nlm.nih.gov/pubmed/3049558 |
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