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 P0ACB2
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.
|
UniProtKB Entries (1)
| P0ACB2 |
HEM2_ECOLI
Escherichia coli K-12
Delta-aminolevulinic acid dehydratase
|
PDB Structure
| PDB | 1I8J |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
Biochemistry
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