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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
porphobilinogen + H2O
hydroxylmethylbilane + NH3
porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
polymerization of 4 pyrrole molecules to a linear tetrapyrrole
i.e. pre-uroporphyrinogen, highly unstable compound
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
porphobilinogen + H2O
uroporphyrinogen III
additional information
?
-
4 porphobilinogen + H2O

hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
-
-
-
?
porphobilinogen

?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
5882, 5883, 489925, 489926, 489935, 489938, 489941, 489942, 489943, 489945, 489948, 489951 -
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen
?
-
-
-
-
-
porphobilinogen + H2O

1-hydroxymethylbilane + 4 NH3
-
third reaction step in heme biosynthesis pathway
-
-
?
porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
-
polymerization of 4 pyrrole molecules to a linear tetrapyrrole
i.e. pre-uroporphyrinogen, highly unstable compound
-
?
porphobilinogen + H2O

hydroxylmethylbilane + NH3
-
-
1-hydroxymethylbilane, highly unstable
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
uroporphyrinogen I
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
uroporphyrinogen I
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
stoichiometry of enzyme reaction
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
HMB
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
PBG
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
uroporphyrinogen I, uroporphyrinogen
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
at pH 8.2, uroporphyrinogen I
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
uroporphyrinogen I
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
at pH 8.2, uroporphyrinogen I
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
uroporphyrinogen
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxylmethylbilane + NH3
-
PBG
-
?
porphobilinogen + H2O

hydroxymethylbilane + NH3
-
-
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
enzyme defects are involved in acute intermittent porphyria, AIP
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
enzyme defects are involved in acute intermittent porphyria, AIP, a neuropathic disease
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
the enzyme is important in heme biosynthesis, a nonsense mutation in the porphobilinogen deaminase gene causes acute intermittent porphyria, AIP, overview, eight enzymes are involved in the heme synthesis and defects in seven of them cause porphyria, overview
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
the enzyme is important in heme biosynthesis, a nonsense mutation in the porphobilinogen deaminase gene causes chester porphyria, existence of dual porphyrias with two enzymes of heme biosynthesis being deficient simultaneously, overview
-
-
?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
third step in the heme biosynthetic pathway, enzyme defects are involved in acute intermittent porphyria, AIP, an autosomal dominant disorder characterised by acute, potentially life-threatening neurological attacks that are precipitated by various drugs, reproductive hormones and other factors
-
-
?
porphobilinogen + H2O

uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
uroporphyrinogen III cosynthase is more heat-labile than porphobilinogen deaminase. Heat-treatment of the porphobilinogen deaminase/uroporphyrinogen III cosynthase enzyme system forms only 2-4% of uroporphyrinogen III
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
-
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
porphobilinogen + H2O
uroporphyrinogen III
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
additional information

?
-
-
third enzyme in the heme biosynthetic pathway
-
-
-
additional information
?
-
-
in presence of a second enzyme, EC 4.2.1.75, uroporphyrinogen-III synthase, often called co-synthase, the product is cyclized to form uroporphyrinogen-III
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additional information
?
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enzyme from chloroplasts is a nuclear-encoded protein, contains a transit-peptide part for transport across the organelle membrans
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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occurrence of multiple forms of the enzyme. These isomers correspond to the enzyme-substrate intermediates: mono-, di-, tri-, and tetrapyrrole
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additional information
?
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mutations of the residues R167, R173, R149, and D99 of the enzyme cause acute intermittent porphyria, overview
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additional information
?
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recurrent mutations G111R and R173Q occurring at CpG motifs of the enzyme cause acute intermittent porphyria AIP, a disorder of the heme biosynthetic pathway, oerview
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additional information
?
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safety, pharmacokinetics and pharmacodynamics of recombinant human porphobilinogen deaminase P 9808, administered to healthy subjects and asymptomatic porphobilinogen deaminase-deficient subjects with high concentrations of porphobilinogen, the substrate of porphobilinogen deaminase for investigation and establishing of an alternative therapy of acute intermittent porphyria, AIP, method, overview
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additional information
?
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the enzyme is also active in uroporphyrinogen formation from porphobilinogen, cf. EC 4.2.1.75
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additional information
?
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enzyme-intermediates with increasing number of porphobilinogen molecules are formed during the catalysis of enzyme HMBS
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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third enzyme in the heme biosynthetic pathway
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
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third reaction step in heme biosynthesis pathway
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?
porphobilinogen + H2O
hydroxymethylbilane + NH3
additional information
?
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4 porphobilinogen + H2O

hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
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?
porphobilinogen

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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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5882, 5883, 489925, 489926, 489935, 489938, 489941, 489942, 489943, 489945, 489948, 489951 -
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porphobilinogen
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen
?
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porphobilinogen + H2O

hydroxymethylbilane + NH3
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enzyme defects are involved in acute intermittent porphyria, AIP
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?
porphobilinogen + H2O
hydroxymethylbilane + NH3
-
enzyme defects are involved in acute intermittent porphyria, AIP, a neuropathic disease
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?
porphobilinogen + H2O
hydroxymethylbilane + NH3
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the enzyme is important in heme biosynthesis, a nonsense mutation in the porphobilinogen deaminase gene causes acute intermittent porphyria, AIP, overview, eight enzymes are involved in the heme synthesis and defects in seven of them cause porphyria, overview
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?
porphobilinogen + H2O
hydroxymethylbilane + NH3
the enzyme is important in heme biosynthesis, a nonsense mutation in the porphobilinogen deaminase gene causes chester porphyria, existence of dual porphyrias with two enzymes of heme biosynthesis being deficient simultaneously, overview
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?
porphobilinogen + H2O
hydroxymethylbilane + NH3
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third step in the heme biosynthetic pathway, enzyme defects are involved in acute intermittent porphyria, AIP, an autosomal dominant disorder characterised by acute, potentially life-threatening neurological attacks that are precipitated by various drugs, reproductive hormones and other factors
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-
?
additional information

?
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third enzyme in the heme biosynthetic pathway
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-
-
additional information
?
-
-
in presence of a second enzyme, EC 4.2.1.75, uroporphyrinogen-III synthase, often called co-synthase, the product is cyclized to form uroporphyrinogen-III
-
-
-
additional information
?
-
-
enzyme from chloroplasts is a nuclear-encoded protein, contains a transit-peptide part for transport across the organelle membrans
-
-
-
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
-
additional information
?
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third enzyme in the heme biosynthetic pathway
-
-
-
additional information
?
-
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third enzyme in the heme biosynthetic pathway
-
-
-
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
-
additional information
?
-
-
occurrence of multiple forms of the enzyme. These isomers correspond to the enzyme-substrate intermediates: mono-, di-, tri-, and tetrapyrrole
-
-
-
additional information
?
-
-
mutations of the residues R167, R173, R149, and D99 of the enzyme cause acute intermittent porphyria, overview
-
-
-
additional information
?
-
-
recurrent mutations G111R and R173Q occurring at CpG motifs of the enzyme cause acute intermittent porphyria AIP, a disorder of the heme biosynthetic pathway, oerview
-
-
-
additional information
?
-
-
safety, pharmacokinetics and pharmacodynamics of recombinant human porphobilinogen deaminase P 9808, administered to healthy subjects and asymptomatic porphobilinogen deaminase-deficient subjects with high concentrations of porphobilinogen, the substrate of porphobilinogen deaminase for investigation and establishing of an alternative therapy of acute intermittent porphyria, AIP, method, overview
-
-
-
additional information
?
-
-
the enzyme is also active in uroporphyrinogen formation from porphobilinogen, cf. EC 4.2.1.75
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
?
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third enzyme in the heme biosynthetic pathway
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additional information
molecular dynamics simulations for determmination of the exit mechanism of hydroxymethylbilane from the enzyme at the end of the catalytic cycle
evolution

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all enzymes in the family adopt a three-domain fold in which domains 1 and 2 resemble the fold of type II periplasmic binding proteins and the third domain, to which the cofactor is covalently attached, adopts a distinct alpha/beta topology
evolution
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all enzymes in the family adopt a three-domain fold in which domains 1 and 2 resemble the fold of type II periplasmic binding proteins and the third domain, to which the cofactor is covalently attached, adopts a distinct alpha/beta topology
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malfunction

half-maximal activity of the enzyme causes acute intermittent porphyria due to an error of heme biosynthesis; half-maximal activity of the enzyme causes acute intermittent porphyria due to an error of heme biosynthesis; half-maximal activity of the enzyme causes acute intermittent porphyria due to an error of heme biosynthesis
malfunction
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acute intermittent porphyria is characterized by a partial deficiency in the enzyme, the third enzyme in heme biosynthesis
malfunction
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mutation causes acute intermittent porphyria
malfunction
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mutations cause acute intermittent porphyria
malfunction
enzyme deficiency results in overproduction of porphyrin precursors in acute intermittent porphyria
malfunction
enzyme deficiency results in overproduction of porphyrin precursors in acute intermittent porphyria
malfunction
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camouflage1 (cf1) mutant develops nonclonal, yellow-green sectors in leaves based on bundle sheath cell-specific death, yellow mutant regions show reduced levels of chlorophyll a + b, and total carotenoids, reduced photosynthesis and stomatal conductance compared to wild type and green regions of the mutant, constant light suppresses the cf1 sector formation, sectors only form during a limited time of leaf development, underlying is a decreased enzyme activity and increased levels of the substrate in green and yellow regions, yellow regions show an additional reduction in catalase activity
malfunction
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autosomal dominantly inherited disease acute intermittent porphyria, AIP, is caused by mutations in hydroxymethylbilane synthase, phenotypes, overview
metabolism

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third enzyme in heme biosynthesis pathway in mammals
metabolism
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third enzyme in heme biosynthesis
metabolism
the enzyme hydroxymethylbilane synthase catalyses a key early step of the heme and chlorophyll biosynthesis pathways in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole
metabolism
the enzyme hydroxymethylbilane synthase catalyses a key early step of tetrapyrrole biosynthesis pathways in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole
metabolism
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hydroxymethylbilane synthase is the third enzyme in the heme biosynthesis pathway
metabolism
porphobilinogen deaminase, an enzyme in the heme biosynthetic pathway, catalyzes the formation of a linear tetrapyrrole product, 1-hydroxymethylbilane, from four units of porphobilinogen
metabolism
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the enzyme hydroxymethylbilane synthase catalyses a key early step of tetrapyrrole biosynthesis pathways in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole; the enzyme hydroxymethylbilane synthase catalyses a key early step of tetrapyrrole biosynthesis pathways in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole
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physiological function

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early step in chlorophyll and heme biosynthesis
physiological function
overproduction of enzyme in Emericella nidulans promotes reactive nitrogen species tolerance, whereas repression causes growth that is hypersensitive to reactive nitrogen species. Hydroxymethylbilane synthase modulates the reduction of environmental NO and nitrite levels by flavohemoglobin and nitrite reductase
physiological function
porphobilinogen deaminase catalyzes the formation of 1-hydroxymethylbilane, a crucial intermediate in tetrapyrrole biosynthesis, through a step-wise polymerization of four molecules of porphobilinogen, using a unique dipyrromethane cofactor
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K55Q/K59Q
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K55Q-K59Q mutant, lower specific activity than the wild-type enzyme
K59Q
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K59Q mutant, lower specific activity than the wild-type enzyme
A84T
type OregonAR (c250G>A), autosomal recessive, therefore phenotype is homozygous, about 35% wild type activity; type OregonAR (c250G>A), autosomal recessive, therefore phenotype is homozygous, about 35% wild type activity; type OregonAR (c250G>A), autosomal recessive, therefore phenotype is homozygous, about 35% wild type activity
L64S
c.189dupT mutant type Saskatchewan with duplication that leads to a frameshift and thus to a trunkated enzyme due to a premature stop codon 65 and the exchange L64S, autosomal dominant; c.189dupT mutant type Saskatchewan with duplication that leads to a frameshift and thus to a trunkated enzyme due to a premature stop codon 65 and the exchange L64S, autosomal dominant; c.189dupT mutant type Saskatchewan with duplication that leads to a frameshift and thus to a trunkated enzyme due to a premature stop codon 65 and the exchange L64S, autosomal dominant
R149W
type Missouris (c.445C>T), substitution identical to human mutation but there leading to an nonsense mutation, autosomal dominant, less than 1% wild type activity; type Missouris (c.445C>T), substitution identical to human mutation but there leading to an nonsense mutation, autosomal dominant, less than 1% wild type activity; type Missouris (c.445C>T), substitution identical to human mutation but there leading to an nonsense mutation, autosomal dominant, less than 1% wild type activity
887insA
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site-directed mutagenesis, the mutant shows reduced expression and subcellular distribution compared to the wild-type enzyme
D99G
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site-directed mutagenesis, inactive holo-enzyme mutant existing as a complex with 2 substrate molecules covalently bound to the dipyrromethane cofactor
G24S
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c.70G>A (p.Gly24Ser)
G748A
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site-directed mutagenesis, the mutant shows reduced expression and subcellular distribution compared to the wild-type enzyme
G748C
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site-directed mutagenesis, the mutant shows reduced expression and subcellular distribution compared to the wild-type enzyme
H300L
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c.899_900delinsTGCCTGCATCTG (p.His300LeuFsX10)
K132N
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site-directed mutagenesis, the mutant shows no conformational or kinetic defect, no loss in relative activity (97% of wild-type activity) at standard conditions nor change in Vmax and Km. The mutation is not associated to acute intermittent porphyria, AIP
N322K
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c.965_966insA (p.Asn322LysfsX36)
Q204K
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c.610C>A, exon 10, missense mutation, 46% wild type activity, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
R116W
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site-directed mutagenesis, the mutant shows 0.5% of wild-type activity and defects in conformational stability. The mutation is associated to acute intermittent porphyria, AIP
R149Q
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site-directed mutagenesis, inactive apo-enzyme which is unable to assemble with the dipyrromethane cofactor, the mutant enzyme is unstable and heat-labile
R149X
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identification of a nonsense mutation in the PBGD gene on chromosome 11q23.3, which harbors the mutations causing acute intermittent porphyria, as the underlying genetic defect in Chester porphyria, phenotype, overview
R167W
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site-directed mutagenesis, the mutant shows 4.2% of wild-type activity and defects in enzyme kinetics associated with a very high Km and decreased Vmax. The mutation is associated to acute intermittent porphyria, AIP
R173Q/Q204K
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R173Q is more severe with a resulting enzyme activity of nearly zero, the Q204K increases the negative effect, particularly on the protein stability, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
R173W
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site-directed mutagenesis, the mutant shows 0.6% of wild-type activity and defects in conformational stability and in enzyme kinetics. The mutation is associated to acute intermittent porphyria, AIP
R26H
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c.77G>A, exon 3, 0.2% wild type activity, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
R325A
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c.972_973insG (p.Arg325AlafsX33)
R32P
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c.95G>C (p.Arg32Pro)
R73Q/Q204K
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a complex monoallelic mutation c.[518G>A; c.610C>A] (p.[Arg173Gln;p.Gln204Lys])
V215E
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site-directed mutagenesis, the mutant shows 30% of wild-type activity and lower conformational stability and probably a perturbed elongation process, also 70% loss in both activity and Vmax. The mutation is associated to acute intermittent porphyria, AIP
V215M
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19.4% residual activity compared to the wild type enzyme
L116K
the specific activity of this recombinant mutant enzyme is 5fold higher than that of the recombinant wild type enzyme, catalyzes the formation of uroporphyrinogen I in addition to uroporphyrinogen III
D44A
specific activity is only about 2% of that of the wild type enzyme
Q200L
mutant lacks the dipyrromethane cofactor and completely loses the catalytic activity
A226P

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c.675delA (p.Ala226ProfsX28)
A226P
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c.675delA, exon 12, 0.05% wild type activity, small deletion leads to stop codon after 28 completely different amino acids compared to wild type, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
E250D

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c.750A>T (p.Glu250Asp)
E250D
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c.750A>T, exon 12, missense mutation, 0.5% wild type activity, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
R167Q

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site-directed mutagenesis, mutation of active site residue, highly reduced activity compared to the wild-type enzyme, formation of stable enzyme-intermediate complexes
R167Q
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8.5% activity, reduced pH optimum from 8.0 to 6.0, accumulates long-lived intermediate complexes
R173Q

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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, the major part of the enzyme exists as apo-enzyme without assembled dipyrromethane cofactor
R173Q
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c.518G>A, exon 10, missense mutation, 0.15% wild type activity, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
R26C

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c.76C>T (p.Arg26Cys)
R26C
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c.76C>T, exon 3, 0.3% wild type activity, 50 mM Tris-HCl, pH 8.2, 0.1% bovine serum albumin, 0.1% Triton, pH 8.2, 37°C, 1 h in the dark
T59I

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80.6% residual activity compared to the wild type enzyme
T59I
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c.176C>T (p.Thr59Ille)
additional information

-
all, six, methionine residues are replaced by SeMet
additional information
4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, accumulation of substrates, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, accumulation of substrates, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, accumulation of substrates, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; 4 distinct mutations cause acute intermittent porphyria in cats, mutant phenotype has brownish discolored teeth and brownish urine, both fluorescent under UV light, mutations affect housekeeping and erythroid-specific isozymes in the same way; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity; type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
-
the mutations of the enzyme cause acute intermittent porphyria
additional information
-
analysis of naturally occurring mutations causing acute intermittent porphyria, e.g. recurrent mutations G111R and R173Q occurring at CpG motifs from different patients, countries of origin, overview, haplotype analysis, polymorphism analysis, microsatellite marker analysis, oerview
additional information
-
identification of a mutation in the porphobilinogen deaminase gene in a Slovak acute intermittent porphyria patient, phenotype, the recombinantly expressed mutant enzyme shows 0.18% of wild-type activity, overview
additional information
-
mutations involved in acute intermittent porphyria, AIP, lead to an inactivation of the mutant enzyme, the mutations influence the structure and function of the enzyme
additional information
-
the commonly known variations g.-64T/C (rs589925), g.3581A/G (rs17075), g.6479T/G (rs1131488), and g.7064C/A (rs1784304) are detected by the high-resolution melting method, and also the identified DNA alternations c.76C>T (p.Arg26Cys), c.77G>A (p.Arg26His), c.95G>C (p.Arg32Pro), c.176C>T (p.Thr59Ille), a complex monoallelic mutation c.[518G>A; c.610C>A] (p.[Arg173Gln;p.Gln204Lys]), c.675delA (p.Ala226ProfsX28), c.750A>T (p.Glu250Asp), c.771+1G>T (r.spl?), c.965_966insA (p.Asn322LysfsX36), and c.972_973insG (p.Arg325AlafsX33) can be identified, additionally the alterations g.2922T>G, g.3059G>A, g.3119T/G (rs1006195), c.70G>A (p.Gly24Ser), c.87+5G>T (r.spl?), c.[518G>A;c.610C>A] (p.[Arg173Gln, p.Gln204Lys]), g.7175A>G, c.899_900delinsTGCCTGCATCTG (p.His300LeuFsX10), g.7998G/A (rs1799997) are identified in 97 subjects
additional information
-
previously known mutations that are identified by molecular analysis of the hydroxymethylbilane synthase gene are c.76C>T (R26Cys), c.77G>A (R26H), c.518G>A (R173Q), c.771 + 1G>T (causing donor splice site defect, deletion of exon 12), novel mutations are c.610C>A (Q204K), c.675delA (A226P with stop codon 28), c.750A>T (E250D), one patient shows double mutation of R173Q and Q204K
additional information
disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
additional information
disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
additional information
-
4 insertion allels (m1-m4) of camouflage1 (cf1) mutant, mutant develops nonclonal, yellow-green sectors in leaves based on bundle sheath cell-specific death, yellow mutant regions show reduced levels of chlorophyll a + b, and total carotenoids, reduced photosynthesis and stomatal conductance compared to wild type and green regions of the mutant, constant light suppresses the cf1 sector formation, sectors only form during a limited time of leaf development, underlying is a decreased enzyme activity and increased levels of the substrate in green and yellow regions, yellow regions show an additional reduction in catalase activity
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5 forms, A: native enzyme, B-E: isomeres corresponding to the enzyme-substrate intermediates
-
blood samples are washed in phosphate buffered saline, liver rinsed in phosphate buffered saline
cell harvesting by centrifugation, washed, resuspended in NaCl-phosphate buffer containing of 140 mN NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH 7.3 with protease inhibitor cocktail, and 0.5% Triton X-100, lysis by shaking with lysozyme on ice, sonication, centrifugation, supernatant loaded onto glutathione sepharose 4B column, washed with 20 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, 0.5% Nonidet P-40+, pH 8.2, proteins eluted in 50 mM Tris-HCl, pH 8.3 buffer with 20 mM glutathione, thrombin digestion with thrombin at 20 U/mg protein at 20°C overnight, addition of glycerol to a concentration of 20%
-
cells centrifuged, washed with 0.9 M NaCl, re-centrifuged, washed with 20 mM Tris-HCl buffer, pH 8.2, with 5 mM dithiothreitol, and 200 microM PMSF, sonication, heating to 60°C under N2 gas, cooled to 4°C, supernatant applied to a Pharmacia 50 K/30 column packed with DEAE-Sephacel anion-exchange resin, equilibrated with 50 mM Tris-HCl buffer, pH 8.2 containing 5 mM dithiothreitol, and 100 microM PMSF, elution with 0-70 mM KCl gradient, active fractions are pooled and concentrated by ultrafiltration with a PM-10 membrane, further concentrated with a Centricon YM-10 centrifugal filter and gel-filtered on a Hiload 16/60 Superdex G-75 column, equilibrated with 100 mM Tris-HCl buffer, pH 8.2, containing 5 mM dithiothreitol and 100 microM PMSF, concentrated with a Centricon YM-10, buffer-exchanged into 20 mM Tris-HCl buffer, pH 8.2, containing 5 mM dithiothreitol with a Pharmacia PD10 column
-
cells harvested and resuspended in 20 mM Tris-HCl buffer, pH 8.0 containing 500 mM NaCl and 10 mM imidazole, cells are lysed by sonication and centrifuged, applied to NiCl2 Sepahrose resin and eluted with buffer and 500 mM imidazole, pooled, concentrated by ultra centrifugation (10 kDa), buffer exchanged with 50 mM Tris-HCl, pH 8.0, with a PD10 column
-
dye-ligand affinity chromatography
-
glutathione Sepharose 4B column chromatography
-
Hi-Trap chelating metal affinity column chromatography
leaves of 8 week old field grown plants are ground in liquid nitrogen and extracted with 25 mM NaP buffer, pH 8.0, containing 1 mM EDTA, 5 mM DTT, and 0.5 mM phenylmethanesulfonylfluoride, centrifuged, supernatant taken for enzyme assay
-
Ni2+-NTA resin chromatography
packed red blood cells are washed in phosphate buffered saline, lysed with buffer containing 0.1 M KHEPES, pH 7.5, 0.1% Triton X-100, 1 mM DTT, and 0.02% sodium azide, liver and spleen are diced and homogenized in buffer containing 50 mM KHEPES, pH 7.5, 150 mM KCl, 1 mM Na2EDTA, 1 mM DTT, 0.1 mM PMSF, for activity and thermostability experiments enzymes are expressed in Escherichia coli, cells are harvested and resuspended in 50 mM HEPES, pH 7.8, 0.5 M NaCl, 5 mM DTT, 330 microg/ml lysozyme, 5 microg/ml DNAse and RNAse, freeze-thawed 3times in dry-ice/ethanol, centrifuged, adjusted to pH 7.4 and 8.0 with NaOH, incubated at 37°C or 50°C for 1 h; packed red blood cells are washed in phosphate buffered saline, lysed with buffer containing 0.1 M KHEPES, pH 7.5, 0.1% Triton X-100, 1 mM DTT, and 0.02% sodium azide, liver and spleen are diced and homogenized in buffer containing 50 mM KHEPES, pH 7.5, 150 mM KCl, 1 mM Na2EDTA, 1 mM DTT, 0.1 mM PMSF, for activity and thermostability experiments enzymes are expressed in Escherichia coli, cells are harvested and resuspended in 50 mM HEPES, pH 7.8, 0.5 M NaCl, 5 mM DTT, 330 microg/ml lysozyme, 5 microg/ml DNAse and RNAse, freeze-thawed 3times in dry-ice/ethanol, centrifuged, adjusted to pH 7.4 and 8.0 with NaOH, incubated at 37°C or 50°C for 1 h; packed red blood cells are washed in phosphate buffered saline, lysed with buffer containing 0.1 M KHEPES, pH 7.5, 0.1% Triton X-100, 1 mM DTT, and 0.02% sodium azide, liver and spleen are diced and homogenized in buffer containing 50 mM KHEPES, pH 7.5, 150 mM KCl, 1 mM Na2EDTA, 1 mM DTT, 0.1 mM PMSF, for activity and thermostability experiments enzymes are expressed in Escherichia coli, cells are harvested and resuspended in 50 mM HEPES, pH 7.8, 0.5 M NaCl, 5 mM DTT, 330 microg/ml lysozyme, 5 microg/ml DNAse and RNAse, freeze-thawed 3times in dry-ice/ethanol, centrifuged, adjusted to pH 7.4 and 8.0 with NaOH, incubated at 37°C or 50°C for 1 h
recombinant enzyme from Escherichia coli by ion exchange chromatography and gel filtration
recombinant GST-tagged isoallelic forms K210 and E210 mutants from Escherichia coli to homogeneity
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli BL21 (DE3) by glutathione affinity chromatography, the GST-tag is cleaved off
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) pLysS by glutathione affinity chromatgraphy, tag cleavage by thrombin, and ultrafiltration
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, removal of the His-tag by thrombin and tag elimination by another step of nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli, removal of the His-tag
-
SeMet-labelled enzyme, i.e. [SeMet] HMBS, and wild-type enzyme
-
-

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partial

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Wright, D.J.; Lim, C.K.
Simultaneous determination of hydroxymethylbilane synthase and uroporphyrinogen III synthase in erythrocytes by high-performance liquid chromatography
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213
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1983
Homo sapiens
brenda
Frydman, R.B.; Feinstein, G.
Studies on porphobilinogen deaminase and uroporphyrinogen III cosynthase from human erythrocytes
Biochim. Biophys. Acta
350
358-373
1974
Homo sapiens
brenda
Jordan, P.M.; Berry, A.
Preuroporphyrinogen, a universal intermediate in the biosynthesis of uroporphyrinogen III
FEBS Lett.
112
86-88
1980
Rhodobacter sphaeroides, Rhodobacter sphaeroides NCIB 8253
brenda
Levin, E.Y.; Coleman, D.L.
The enzymatic conversion of porphobilinogen to uroporphyrinogen catalyzed by extracts of hematopoietic mouse spleen
J. Biol. Chem.
242
4248-4253
1967
Mus musculus, Spinacia oleracea
-
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Jordan, P.M.; Shemin, D.
Purification and properties of uroporphyrinogen I synthetase from Rhodopseudomonas spheroides
J. Biol. Chem.
248
1019-1024
1973
Rhodobacter sphaeroides
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Davies, R.C.; Neuberger, A.
Polypyrroles formed from porphobilinogen and amines by uroporphyrinogen synthetase of Rhodopseudomonas spheroides
Biochem. J.
133
471-492
1973
Bos taurus, Glycine max, Rhodobacter sphaeroides, Rhodobacter sphaeroides NCIB 8253, Spinacia oleracea, Triticum aestivum
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Miyagi, K.; Kaneshima, M.; Kawakami, J.; Nakada, F.; Petryka, Z.J.; Watson, C.J.
Uroporphyrinogen I synthetase from human erythrocytes: Separation, purification, and properties of isoenzymes
Proc. Natl. Acad. Sci. USA
76
6172-6176
1979
Bos taurus, Homo sapiens, Rhodobacter sphaeroides, Spinacia oleracea
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Anderson, P.M.; Desnick, R.J.
Purification and properties of uroporphyrinogen I synthase from human erythrocytes
J. Biol. Chem.
255
1993-1999
1980
Homo sapiens
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Battersby, A.R.; Fookes, C.J.R.; Matcham, G.W.J.; McDonald, E.
Biosynthesis of the pigments of life: formation of the macrocycle
Nature
285
17-19
1980
Euglena gracilis, Gallus gallus, Propionibacterium freudenreichii subsp. shermanii
brenda
Shioi, Y.; Nagamine, M.; Kuroki, M.; Sasa, T.
Purification by affinity chromatography and properties of uroporphyrinogen I synthetase from Chlorella regularis
Biochim. Biophys. Acta
616
300-309
1980
Chlorella regularis, Chlorella regularis S-50, Rhodobacter sphaeroides, Spinacia oleracea, Triticum aestivum
brenda
Russell, C.S.; Rockwell, P.
The effects of sulfhydryl reagents on the activity of wheat germ uroporphyrinogen I synthase
FEBS Lett.
116
199-202
1980
Triticum aestivum
brenda
Williams, D.C.; Morgan, G.S.; McDonald, E.; Battersby, A.R.
Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics
Biochem. J.
193
301-310
1981
Euglena gracilis
brenda
Williams, D.C.
Characterization of the multiple forms of hydroxymethylbilane synthase from rat spleen
Biochem. J.
217
675-683
1984
Rattus norvegicus
brenda
Farmer, D.J.; Hollebone, B.R.
Comparative inhibition of hepatic hydroxymethylbilane synthase by both hard and soft metal cations
Can. J. Biochem. Cell Biol.
62
49-54
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Brown, R.C.; Elder, G.H.; Urquhart, A.J.
Purification of hydroxymethylbilane synthase from human erythrocytes
Biochem. Soc. Trans.
13
1227-1228
1985
Homo sapiens
-
brenda
Helliwell, J.R.; Nieh, Y.P.; Raftery, J.; Cassata, A.; Habash, J.; Carr, P.D.; Ursby, T.; Wulff, M.; Thompson, A.W.; Niemann, A.C.; Haedener, A.
Time-resolved structures of hydroxymethylbilane synthase (Lys59Gln mutant) as it is loaded with substrate in the crystal determined by Laue diffraction
J. Chem. Soc. Faraday Trans.
94
2615-2622
1998
Escherichia coli
-
brenda
Hart, G.J.; Abell, C.; Battersby, A.R.
Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli
Biochem. J.
240
273-276
1986
Escherichia coli
brenda
Mazzetti, M.B.; Tomio, J.M.
Purification and some properties of rat liver uroporphyrinogen I synthase
Anal. Asoc. Quim. Argent.
76
207-215
1988
Chlorella regularis, Escherichia coli, Homo sapiens, Rattus norvegicus, Spinacia oleracea
-
brenda
Miller, A.D.; Hart, G.J.; Packman, L.C.; Battersby, A.R.
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242
Biochem. J.
254
915-918
1988
Escherichia coli, Escherichia coli TG1
brenda
Beifuss, U.; Hart, G.J.; Miller, A.D.; Battersby, A.R.
13C-N.M.R. Studies on the pyrromethane cofactor of hydroxymethylbilane synthase
Tetrahedron Lett.
29
2591-2594
1988
Escherichia coli
-
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Smythe, E.; Williams, D.C.
A simple rapid purification scheme for hydroxymethylbilane synthase from human erythrocytes
Biochem. J.
251
237-241
1988
Homo sapiens
brenda
Lannfelt, L.; Wetterberg, L.; Lilius, L.; Thunell, S.; Joernvall, H.; Pavlu, B.; Wielburski, A.; Gellerfors, P.
Porphobilinogen deaminase in human erythrocytes
Scand. J. Clin. Lab. Invest.
49
677-684
1989
Homo sapiens
brenda
Sharif, A.; Smith, A.G.; Abell, C.
Isolation and characterisation of cDNA clone for chlorophyll synthesis enzyme from Euglena gracilis
Eur. J. Biochem.
184
353-359
1989
Escherichia coli, Euglena gracilis, Homo sapiens, Rattus norvegicus
brenda
Haedener, A.; Alefounder, P.; Hart, G.J.; Abell, C.; Battersby, A.R.
Investigation of putative active-site lysine residues in C
Biochem. J.
271
487-491
1990
Escherichia coli
brenda
Corrigall, A.V.; Meissner, P.N.; Kirsch, R.E.
Purification of human erythrocyte porphobilinogen deaminase
S. Afr. Med. J.
80
294-269
1991
Homo sapiens
brenda
Spano, A.J.; Timko, M.P.
Isolation, characterization and partial amino acid sequence of a chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.)
Biochim. Biophys. Acta
1076
29-36
1991
Glycine max, Pisum sativum
brenda
Jordan, P.M; Warren, M.J.; Mgbeje, B.I.A.; Wood, S.P.; Cooper, J.B.; Louie, G.; Brownlie, P.; Lambert, R.; Blundell, T.L.
Crystallization and preliminary X-ray investigation of Escherichia coli porphobilinogen deaminase.
J. Mol. Biol.
224
269-271
1992
Escherichia coli
brenda
Meissner, P.; Adams, P.; Kirsch, R.
Allosteric inhibition of human lymphoblast and purified porphobilinogen deaminase by protoporphyrinogen and coproporphyrinogen
J. Clin. Invest.
91
1436-1444
1993
Homo sapiens
brenda
Haedener, A.; Matzinger, P.K.; Malashkevich, V.N.; Louie, G.V.; Wood, S.P.; Oliver, P.; Alefounder, P.R.; Pitt, A.R.; Abell, C.; Battersby, A.R.
Purification, characterization, crystallisation and X-ray analysis of selenomethionine-labelled hydroxymethylbilane synthase from Escherichia coli
Eur. J. Biochem.
211
615-624
1993
Escherichia coli
brenda
Araujo, L.S.; Lombardo, M.E.; Batlle, A.M.D.C.
Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
Int. J. Biochem.
26
1377-1381
1994
Saccharomyces cerevisiae
brenda
Juknat, A.A.; Doernemann, D.; Senger, H.
Purification and kinetic studies on a porphobilinogen deaminase from the unicellular green alga Scenedesmus obliquus
Planta
193
123-130
1994
Chlorella regularis, Escherichia coli, Euglena gracilis, Homo sapiens, Pisum sativum, Rattus norvegicus, Rhodobacter sphaeroides, Saccharomyces cerevisiae, Spinacia oleracea, Tetradesmus obliquus
-
brenda
Jones, R.M.; Jordan, P.M.
Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana
Biochem. J.
299
895-902
1994
Arabidopsis thaliana
-
brenda
Cardalda, C.A.; Juknat, A.A.; Princ, F.G.; Batlle, A.
Rat harderian gland porphobilinogen deaminase: characterization studies and regulatory action of protoporphyrin IX
Arch. Biochem. Biophys.
347
69-77
1997
Rattus norvegicus
brenda
Shoolingin-Jordan, P.M.; Al-Dbass, A.; McNeill, L.A.; Sarwar, M.; Butler, D.
Human porphobilinogen deaminase mutations in the investigation of the mechanism of dipyrromethane cofactor assembly and tetrapyrrole formation
Biochem. Soc. Trans.
31
731-735
2003
Homo sapiens
brenda
Schneider-Yin, X.; Hergersberg, M.; Schuurmans, M.M.; Gregor, A.; Minder, E.I.
Mutation hotspots in the human porphobilinogen deaminase gene: recurrent mutations G111R and R173Q occurring at CpG motifs
J. Inherit. Metab. Dis.
27
625-631
2004
Homo sapiens
brenda
Gruenberg-Etkovitz, N.; Greenbaum, L.; Grinblat, B.; Malik, Z.
Proteasomal degradation regulates expression of porphobilinogen deaminase (PBGD) mutants of acute intermittent porphyria
Biochim. Biophys. Acta
1762
819-827
2006
Homo sapiens
brenda
Sardh, E.; Rejkjaer, L.; Andersson, D.E.; Harper, P.
Safety, pharmacokinetics and pharmocodynamics of recombinant human porphobilinogen deaminase in healthy subjects and asymptomatic carriers of the acute intermittent porphyria gene who have increased porphyrin precursor excretion
Clin. Pharmacokinet.
46
335-349
2007
Homo sapiens
brenda
Poblete-Gutierrez, P.; Wiederholt, T.; Martinez-Mir, A.; Merk, H.F.; Connor, J.M.; Christiano, A.M.; Frank, J.
Demystification of Chester porphyria: a nonsense mutation in the porphobilinogen deaminase gene
Physiol. Res.
55 Suppl 2
S137-S144
2006
Homo sapiens (P08397)
brenda
Ulbrichova, D.; Flachsova, E.; Hrdinka, M.; Saligova, J.; Bazar, J.; Raman, C.S.; Martasek, P.
De Novo mutation found in the porphobilinogen deaminase gene in Slovak acute intermittent porphyria patient: molecular biochemical study
Physiol. Res.
55 Suppl 2
S145-S154
2006
Homo sapiens
brenda
Brons-Poulsen, J.; Christiansen, L.; Petersen, N.E.; Horder, M.; Kristiansen, K.
Characterization of two isoalleles and three mutations in both isoforms of purified recombinant human porphobilinogen deaminase
Scand. J. Clin. Lab. Invest.
65
93-105
2005
Homo sapiens
brenda
Wang, Y.; Scott, C.R.; Gelb, M.H.; Turecek, F.
Direct assay of enzymes in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry. Porphobilinogen deaminase
Anal. Chem.
80
2606-2611
2008
Homo sapiens, Homo sapiens (P08397)
brenda
Yang, C.C.; Kuo, H.C.; You, H.L.; Wang, J.; Huang, C.C.; Liu, C.Y.; Lan, M.Y.; Stephenson, D.A.; Lee, M.J.
HMBS mutations in Chinese patients with acute intermittent porphyria
Ann. Hum. Genet.
72
683-686
2008
Homo sapiens
brenda
Li, N.; Chu, X.; Wu, L.; Liu, X.; Li, D.
Functional studies of rat hydroxymethylbilane synthase
Bioorg. Chem.
36
241-251
2008
Rattus norvegicus (P19356)
brenda
Nagaraj, V.A.; Arumugam, R.; Gopalakrishnan, B.; Jyothsna, Y.S.; Rangarajan, P.N.; Padmanaban, G.
Unique properties of Plasmodium falciparum porphobilinogen deaminase
J. Biol. Chem.
283
437-444
2008
Plasmodium falciparum (A8CBH8), Plasmodium falciparum