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. 1986 Nov 15;240(1):273–276. doi: 10.1042/bj2400273

Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.

G J Hart, C Abell, A R Battersby
PMCID: PMC1147405  PMID: 3548707

Abstract

Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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