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 Q59334
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)

Q59334
HEM2_CHLP8
Chlorobaculum parvum NCIB 8327
Delta-aminolevulinic acid dehydratase

PDB Structure

PDB 1W1Z
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution.
Coates, L., Beaven, G., Erskine, P.T., Beale, S.I., Avissar, Y.J., Gill, R., Mohammed, F., Wood, S.P., Shoolingin-Jordan, P., Cooper, J.B.
J. Mol. Biol.
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