| EC |
4.2.1.24 |
| Accepted name: |
porphobilinogen synthase |
| Reaction: |
2 5-aminolevulinate = porphobilinogen + 2 H2O |
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For diagram of the early stages of porphyrin biosynthesis, click here |
| 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) |
| Systematic name: |
5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing; porphobilinogen-forming) |
| Comments: |
The fungal enzyme is a metalloprotein. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, METACYC, PDB, CAS registry number: 9036-37-7 |
| References: |
| 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. [PMID: 5773436] |
| 3. |
Yamasaki, H. and Moriyama, T. δ-Aminolevulinic acid dehydratase of Mycobacterium phlei. Biochim. Biophys. Acta 227 (1971) 698–705. [PMID: 4998716] |
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| [EC 4.2.1.24 created 1961] |
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