Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AG-K-12950 3-[5-[[5-(aminomethyl)-3-(2- carboxyethyl)...

Synonyms: AC1L4PRT, AC1Q5VHC, CTK4G3013, AR-1F1117, AR-1F1118, ...

Miller, A.D. et al., Hart, G.J. et al.

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Disease relevance of Pyrromethane cofactor

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] [1].

High impact information on Pyrromethane cofactor

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242 [2].
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] [2].

References

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue. Hart, G.J., Miller, A.D., Battersby, A.R. Biochem. J. (1988) [Pubmed]
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242. Miller, A.D., Hart, G.J., Packman, L.C., Battersby, A.R. Biochem. J. (1988) [Pubmed]

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