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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

Engineering

Engineering on EC 4.2.1.24 - porphobilinogen synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H10F
-
mutant enzyme is active but is not inhibited by zinc. H10F binds a catalytic zinc at 0.5/subunit and binds a second nonessential and noninhibitory zinc at 0.5/subunit
K195A
-
mutant enzyme with only 0.1% of the wild-type activity
K195C
-
mutant enzyme with only 0.1% of the wild-type activity, 2-bromethylamine results in recovery of 10% of the wild-type activity
K247A
-
inactive mutant enzyme
K247C
-
inactive mutant enzyme, 2-bromethylamine results in recovery of 6% of the wild-type activity
A274K
naturally occurring ALAD porphyria-associated human PBGS mutants are shown to have an increased susceptibility to inhibition by both N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
C132R
-
enzyme activity undetectable
G133R
-
11% of wild-type activity
K59N
-
112% of wild-type activity
K59N/G133R
-
22% of wild-type activity
L273R
-
enzyme activity undetectable
R221K
mutation in wild-type or chimeric enzymes reduces activity
R240A
mutant enzyme assembles into a metastable hexamer, which can undergo a reversible conversion to the octamer in the presence of substrate
R240AS
metastable nature of the R240A hexamer
V153M
-
about 67% of wild-type activity
W19A
assembles into a mixture of stable dimers
C326A
-
no effect on enzymatic activity
DELTA646-658
-
a mutant enzyme lacking the C-terminal 13 amino acids distinguishing parasite PBGS from plant and animal enzymes is purified as a dimer, suggesting that the C-terminus is required for octamer stabilisation
additional information