CATH Classification

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.

UniProtKB Entries (1)

Q59643
HEM2_PSEAE
Pseudomonas aeruginosa PAO1
Delta-aminolevulinic acid dehydratase

PDB Structure

PDB 1GZG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism.
Frere, F., Schubert, W.D., Stauffer, F., Frankenberg, N., Neier, R., Jahn, D., Heinz, D.W.
J. Mol. Biol.