CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.20 | Alpha-Beta Barrel | |
3.20.20 | TIM Barrel | |
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
Superfamily | Aldolase class I |
Functional Family | Delta-aminolevulinic acid dehydratase |
Enzyme Information
4.2.1.24 |
Porphobilinogen synthase.
based on mapping to UniProt Q59643
2 5-aminolevulinate = porphobilinogen + 2 H(2)O.
-!- The enzyme catalyzes 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. -!- 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.
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UniProtKB Entries (1)
Q59643 |
HEM2_PSEAE
Pseudomonas aeruginosa PAO1
Delta-aminolevulinic acid dehydratase
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PDB Structure
PDB | 1W54 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Tracking the Evolution of Porphobilinogen Synthase Metal Dependence in Vitro
J.Mol.Biol.
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