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

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...

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Autori principali: Hart, G J, Miller, A D, Battersby, A R
Natura: Artigo
Lingua:Inglês
Pubblicazione: 1988
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1149235/
https://ncbi.nlm.nih.gov/pubmed/3421931
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