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4.2.1.24: porphobilinogen synthase

This is an abbreviated version!
For detailed information about porphobilinogen synthase, go to the full flat file.

Word Map on EC 4.2.1.24

Reaction

2 5-aminolevulinate =

porphobilinogen
+ 2 H2O

Synonyms

5-aminolaevulinic acid dehydratase, 5-aminolevulinate dehydrase, 5-aminolevulinate dehydratase, 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), 5-aminolevulinic acid dehydrase, 5-aminolevulinic acid dehydratase, 5-levulinic acid dehydratase, Al-D, ALA dehydratase, ALA synthetase, ALA-D, ALAD, ALADH, aminolevulinate dehydrase, aminolevulinate dehydratase, aminolevulinic dehydratase, CF-2, d-ALAD, delta aminolevulinic acid dehydratase, delta-ALA-D, delta-ALAD, delta-aminolevulinate dehydrase, delta-aminolevulinate dehydratase, delta-aminolevulinate dehydrataseALAD, delta-aminolevulinic acid dehydrase, delta-aminolevulinic acid dehydratase, delta-aminolevulinic dehydratase, gamma-aminolevulinic acid dehydratase, HemB, PaPBGS, PBG synthase, PBG-S, PBG-synthase, PBGS, Pcal_1709, PfALAD, PGBS, Porphobilinogen synthase, porphobilinogen synthetase, synthase, porphobilinogen, TgPBGS

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.24 porphobilinogen synthase

Crystallization

Crystallization on EC 4.2.1.24 - porphobilinogen synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid
high-resolution structure of the enzyme cocrystallized with a noncovalently bound moiety of the product, porphobilinogen. The pyrrole side-chain amino group is datively bound to the active-site zinc ion and the porphobilinogen carboxylates interact with the enzyme via hydrogen bonds and salt bridges with invariant residues. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
X-ray structure of the enzyme complexed with the inhibitor levulinic acid at 2.0 A resolution
sitting-drop vapour-diffusion method
two monomers per asymmetric unit. In native human ALAD, the A monomer has a ligand resembling the substrate 5-aminolaevulinic acid which is covalently bound by a Schiff base to active-site Lys252 and is held in place by an ordered active-site loop. These features of the active-site structure are disordered or absent in the B subunit. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
hanging drop method, enzyme complexed with the inhibitor laevulinic acid at 2.6 A resolution, unit cell parameters: a = 125.24 A, b = 125.24 A, c = 164.6 A and spec group P42(1)2
-
hanging drop vapor-diffusion method. Crystal structures of the active site of Pseudomonas aeruginosa PBGS with the various inhibitors 5-hydroxylevulinic acid, 5,5'-oxybis(4-oxopentanoic acid), 5,5'-iminobis(4-oxopentanoic acid), 5,5'-thiobis(4-oxopentanoic acid), 5,5'-sulfinylbis(4-oxopentanoic acid) or 5,5'-sulfonylbis(4-oxopentanoic acid)
hanging drop vapour diffusion method, crystals of the enzyme complex with levulinic acid solved at 1.67 A resolution, crystals belong to space group P42(1)2 with cell dimensions of a = b = 129.8 A, c = 86.7 A
-
porphobilinogen synthase is cocrystallized with the alaremycin
structure of the active-site variant D139N of the Mg2+-dependent enzyme in complex with the inhibitor 5-fluorolevulinic acid
to 3.5 A resolution. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
hanging-drop vapour diffusion method, X-ray structure of the enzyme in which the catalytic site of the enzyme is complexed with a putative cyclic intermediate composed of both substrate moieties, solved at 0.16 nm resolution
the X-ray structure of the enzyme complexed with the competitive inhibitor 5-hydroxylaevulinic acid, determined at a 1.9 A resolution