CATH Domain 1l6yB00

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	1L6Y
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Species-Specific Inhibition of Porphobilinogen Synthase by 4-Oxosebacic Acid Jaffe, E.K., Kervinen, J., Martins, J., Stauffer, F., Neier, R., Wlodawer, A., Zdanov, A. J.Biol.Chem.

Network disruptions