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 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 5MHB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Mills-Davies, N., Butler, D., Norton, E., Thompson, D., Sarwar, M., Guo, J., Gill, R., Azim, N., Coker, A., Wood, S.P., Erskine, P.T., Coates, L., Cooper, J.B., Rashid, N., Akhtar, M., Shoolingin-Jordan, P.M.
Acta Crystallogr D Struct Biol