The Enzyme Database

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Accepted name: porphobilinogen synthase
Reaction: 2 5-aminolevulinate = porphobilinogen + 2 H2O
For diagram of porphyrin biosynthesis (early stages), click here
Glossary: 5-aminolevulinate = δ-aminolevulinate
Other name(s): aminolevulinate dehydratase; δ-aminolevulinate dehydratase; δ-aminolevulinic acid dehydrase; δ-aminolevulinic acid dehydratase; aminolevulinic dehydratase; δ-aminolevulinic dehydratase; 5-levulinic acid dehydratase; 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing); hemB (gene name)
Systematic name: 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing; porphobilinogen-forming)
Comments: The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+ at the active site. In humans, the enzyme is a primary target for the environmental toxin Pb. The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-37-7
1.  Gibson, K.D., Neuberger, A. and Scott, J.J. The purification and properties of δ-aminolaevulic acid dehydrase. Biochem. J. 61 (1955) 618–629. [PMID: 13276347]
2.  Komai, H. and Neilands, J.B. The metalloprotein nature of Ustilago δ-aminolevulinate dehydratase. Biochim. Biophys. Acta 171 (1969) 311–320. [DOI] [PMID: 5773436]
3.  Yamasaki, H. and Moriyama, T. δ-Aminolevulinic acid dehydratase of Mycobacterium phlei. Biochim. Biophys. Acta 227 (1971) 698–705. [DOI] [PMID: 4998716]
4.  Mitchell, L.W. and Jaffe, E.K. Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II). Arch. Biochem. Biophys. 300 (1993) 169–177. [DOI] [PMID: 8424649]
5.  Jaffe, E.K., Ali, S., Mitchell, L.W., Taylor, K.M., Volin, M. and Markham, G.D. Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase. Biochemistry 34 (1995) 244–251. [PMID: 7819203]
6.  Warren, M.J., Cooper, J.B., Wood, S.P. and Shoolingin-Jordan, P.M. Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase. Trends Biochem. Sci. 23 (1998) 217–221. [DOI] [PMID: 9644976]
7.  Jaffe, E.K. and Lawrence, S.H. Allostery and the dynamic oligomerization of porphobilinogen synthase. Arch. Biochem. Biophys. 519 (2012) 144–153. [DOI] [PMID: 22037356]
8.  Tian, B.X., Erdtman, E. and Eriksson, L.A. Catalytic mechanism of porphobilinogen synthase: the chemical step revisited by QM/MM calculations. J. Phys. Chem. B 116 (2012) 12105–12112. [DOI] [PMID: 22974111]
[EC created 1961]

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