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4 porphobilinogen
uroporphyrinogen III + 4 NH3
4 porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
additional information
?
-
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
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
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
-
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
-
third reaction step in heme biosynthesis pathway
-
-
?
4 porphobilinogen + H2O
1-hydroxymethylbilane + 4 NH3
-
polymerization of 4 pyrrole molecules to a linear tetrapyrrole
i.e. pre-uroporphyrinogen, highly unstable compound
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
1-hydroxymethylbilane, highly unstable
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
at pH 8.2, uroporphyrinogen I
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
uroporphyrinogen I
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
at pH 8.2, uroporphyrinogen I
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
uroporphyrinogen I
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
uroporphyrinogen I
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
stoichiometry of enzyme reaction
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
HMB
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
PBG
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
uroporphyrinogen I, uroporphyrinogen
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
uroporphyrinogen
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
-
-
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
-
PBG
-
?
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
-
polymerization of 4 pyrrole molecules to a linear tetrapyrrole
i.e. pre-uroporphyrinogen, highly unstable compound
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
enzyme defects are involved in acute intermittent porphyria, AIP
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
-
enzyme defects are involved in acute intermittent porphyria, AIP, a neuropathic disease
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 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
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 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
-
-
?
4 porphobilinogen + H2O
hydroxymethylbilane + 4 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
-
-
?
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
?
-
-
-
-
?
porphobilinogen
?
-
-
-
-
?
porphobilinogen
?
-
-
5882, 5883, 489925, 489926, 489935, 489938, 489941, 489942, 489943, 489945, 489948, 489951 -
-
?
porphobilinogen
?
-
-
-
-
?
porphobilinogen
?
-
-
-
-
?
porphobilinogen
?
-
-
-
-
?
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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additional information
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third enzyme in the heme biosynthetic pathway
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additional information
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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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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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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
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
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
887insA
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site-directed mutagenesis, the mutant shows reduced expression and subcellular distribution compared to the wild-type enzyme
A31P
0.6% of wild-type activity
A31T
0.50% of wild-type activity
D99H
3.3% of wild-type activity
G218R
0.1% of wild-type activity
G24S
c.70G>A (p.Gly24Ser)
G748A
-
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
c.899_900delinsTGCCTGCATCTG (p.His300LeuFsX10)
K132N
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
K98R
0.70% of wild-type activity
L170R
0.6% of wild-type activity
L170V
72.6% of wild-type activity
N169I
6.2% of wild-type activity
N322K
c.965_966insA (p.Asn322LysfsX36)
Q204K
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
Q34K
0.2% of wild-type activity
Q34R
0.7% of wild-type activity
Q356E
95.7% of wild-type activity
R116W
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
R149L
0.1% of wild-type activity
R149X
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
R150I
0.02% of wild-type activity
R150Q
0.8% of wild-type activity
R173Q/Q204K
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
R195C
3% of wild-type activity
R325A
c.972_973insG (p.Arg325AlafsX33)
R32P
c.95G>C (p.Arg32Pro)
R73Q/Q204K
a complex monoallelic mutation c.[518G>A; c.610C>A] (p.[Arg173Gln;p.Gln204Lys])
S146C
69.9% of wild-type activity
S146G
81% of wild-type activity
S146I
2.3% of wild-type activity
S147P
0.2% of wild-type activity
S165C
69.9% of wild-type activity
S262C
46.3% of wild-type activity
S28C
1.2% of wild-type activity
S28N
0.8 % of wild-type activity
S96F
1.0 % of wild-type activity
T145I
0.4% of wild-type activity
T145N
0.8% of wild-type activity
T58I
0.70% of wild-type activity
V215E
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
c.675delA (p.Ala226ProfsX28)
A226P
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
D99G
3.2% of wild-type activity
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
E250D
c.750A>T (p.Glu250Asp)
E250D
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
R149Q
0.5% of wild-type activity
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
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
8.5% activity, reduced pH optimum from 8.0 to 6.0, accumulates long-lived intermediate complexes
R167Q
1.0% of wild-type activity
R167W
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
R167W
2.3% of wild-type activity
R173Q
0.4% of wild-type activity
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
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
R173W
0.7% of wild-type activity
R173W
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
R26C
0.3% of wild-type activity
R26C
c.76C>T (p.Arg26Cys)
R26C
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
R26H
0.3% of wild-type activity
R26H
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
T59I
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80.6% residual activity compared to the wild type enzyme
T59I
c.176C>T (p.Thr59Ille)
additional information
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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
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
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
additional information
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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
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, mutations affect housekeeping and erythroid-specific isozymes in the same way
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, mutations affect housekeeping and erythroid-specific isozymes in the same way
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, mutations affect housekeeping and erythroid-specific isozymes in the same way
additional information
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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
additional information
type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
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type Massachusetts, in-frame 3 bp deletion (c.842_844delGAG = delGly281), autosomal dominant, less than 1% wild type activity
additional information
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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
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the mutations of the enzyme cause acute intermittent porphyria
additional information
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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
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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
disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
additional information
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disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
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
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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
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
disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
additional information
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disruption in one allele and partial disruption of other allele lead to 25-30% activity compared to wild type
additional information
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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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Wright, D.J.; Lim, C.K.
Simultaneous determination of hydroxymethylbilane synthase and uroporphyrinogen III synthase in erythrocytes by high-performance liquid chromatography
Biochem. J.
213
85-88
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
Cereibacter sphaeroides, Cereibacter 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
-
brenda
Jordan, P.M.; Shemin, D.
Purification and properties of uroporphyrinogen I synthetase from Rhodopseudomonas spheroides
J. Biol. Chem.
248
1019-1024
1973
Cereibacter sphaeroides
brenda
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, Cereibacter sphaeroides, Spinacia oleracea, Triticum aestivum, Cereibacter sphaeroides NCIB 8253
brenda
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, Cereibacter sphaeroides, Homo sapiens, Spinacia oleracea
brenda
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
brenda
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
Gallus gallus, Euglena gracilis, 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, Cereibacter sphaeroides, Spinacia oleracea, Triticum aestivum, Chlorella regularis S-50
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
-
brenda
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
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Homo sapiens
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Homo sapiens
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Homo sapiens (P08397)
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Homo sapiens
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Characterization of two missense variants in the hydroxymethylbilane synthase gene in the Israeli population, which differ in their associations with acute intermittent porphyria
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Homo sapiens
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Homo sapiens (P08397)
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Homo sapiens (P08397), Homo sapiens
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Zhou, S.; Narukami, T.; Nameki, M.; Ozawa, T.; Kamimura, Y.; Hoshino, T.; Takaya, N.
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Aspergillus nidulans (C8VQK3), Aspergillus nidulans
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Insights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzyme
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Arabidopsis thaliana (Q43316), Arabidopsis thaliana
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Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution
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Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
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Priestia megaterium (D5DT75), Priestia megaterium, Priestia megaterium ATCC 12872 (D5DT75)
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Bustad, H.; Vorland, M.; Roenneseth, E.; Sandberg, S.; Martinez, A.; Toska, K.
Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria
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Homo sapiens (P08397)
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Bung, N.; Pradhan, M.; Srinivasan, H.; Bulusu, G.
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Escherichia coli (P06983), Escherichia coli
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Chakrabarty, B.; Das, D.; Bung, N.; Roy, A.; Bulusu, G.
Network analysis of hydroxymethylbilane synthase dynamics
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Homo sapiens (P08397), Homo sapiens
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Bung, N.; Roy, A.; Priyakumar, U.D.; Bulusu, G.
Computational modeling of the catalytic mechanism of hydroxymethylbilane synthase
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Homo sapiens (P08397), Homo sapiens
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Bung, N.; Roy, A.; Chen, B.; Das, D.; Pradhan, M.; Yasuda, M.; New, M.I.; Desnick, R.J.; Bulusu, G.
Human hydroxymethylbilane synthase Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP
Proc. Natl. Acad. Sci. USA
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Homo sapiens (P08397), Homo sapiens
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