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dipyrromethane cofactor

Known as: pyrromethane cofactor 
 
National Institutes of Health

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Porphobilinogen

Papers overview

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2017
2017
Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.
The enzyme porphobilinogen deaminase (PBGD) is one of the key enzymes in tetrapyrrole biosynthesis. It catalyses the formation of… Expand
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2014
2014
Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic…
The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses a key early step in the… Expand
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Highly Cited
1987
Highly Cited
1987
Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase.
Porphobilinogen deaminase isolated from Escherichia coli is shown to contain a dipyrromethane cofactor (DPMC) linked covalently… Expand
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