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

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Gene Review:

hemC - porphobilinogen deaminase

Rhodobacter sphaeroides 2.4.1

Hart, G.J. et al., Jordan, P.M. et al., Moskvin, O.V. et al.

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Disease relevance of hemC

Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides [1].

High impact information on hemC

Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue [2].
When hydroxymethylbilane synthase (porphobilinogen deaminase) from Euglena gracilis is incubated with pyridoxal 5'-phosphate at pH 7.0 and 0 degree C, it rapidly loses part of its activity [2].
In addition to photosystem genes, the hemC and hemE genes involved in the early steps of tetrapyrrole biosynthesis were identified as new direct targets of PpsR repression [3].

References

Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides. Jordan, P.M., Berry, A. Biochem. J. (1981) [Pubmed]
Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue. Hart, G.J., Leeper, F.J., Battersby, A.R. Biochem. J. (1984) [Pubmed]
Transcriptome analysis of the Rhodobacter sphaeroides PpsR regulon: PpsR as a master regulator of photosystem development. Moskvin, O.V., Gomelsky, L., Gomelsky, M. J. Bacteriol. (2005) [Pubmed]

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