CATH Classification

Domain Context

CATH Clusters

Superfamily Aldolase class I
Functional Family Delta-aminolevulinic acid dehydratase

Enzyme Information
Porphobilinogen synthase.
based on mapping to UniProt P05373
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)

Saccharomyces cerevisiae S288C
Delta-aminolevulinic acid dehydratase

PDB Structure

External Links
Organism Escherichia
Primary Citation
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
Erskine, P.T., Senior, N., Awan, S., Lambert, R., Lewis, G., Tickle, I.J., Sarwar, M., Spencer, P., Thomas, P., Warren, M.J., Shoolingin-Jordan, P.M., Wood, S.P., Cooper, J.B.