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Porphobilinogen Deaminase: Methods and Principles of the Enzymatic Assay
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Porphobilinogen (PBG) deaminase catalyzes the formation of the linear tetrapyrrole,
hydroxymethylbilane, from four molecules of PBG. The tetrapyrrole is either converted
to uroporphyrinogen III by uroporphyrinogen cosynthetase or nonenzymatically cyclized to
uroporphyrinogen I. Methods for the biosynthesis of gram quantities of PBG and for the
determination of PBG-deaminase specific activity in various tissues were developed. Using
this assay, the PBG-deaminase activities in human erythrocytes, brain, liver and cultured
fibroblasts and lymphoblasts as well as various rat tissues were determined as reference values.
In addition, the conditions for the use of this assay in the enzymatic diagnosis of heterozygotes
for acute intermittent porphyria were established.
Title: Porphobilinogen Deaminase:
Methods and Principles of the Enzymatic Assay
Description:
Porphobilinogen (PBG) deaminase catalyzes the formation of the linear tetrapyrrole,
hydroxymethylbilane, from four molecules of PBG.
The tetrapyrrole is either converted
to uroporphyrinogen III by uroporphyrinogen cosynthetase or nonenzymatically cyclized to
uroporphyrinogen I.
Methods for the biosynthesis of gram quantities of PBG and for the
determination of PBG-deaminase specific activity in various tissues were developed.
Using
this assay, the PBG-deaminase activities in human erythrocytes, brain, liver and cultured
fibroblasts and lymphoblasts as well as various rat tissues were determined as reference values.
In addition, the conditions for the use of this assay in the enzymatic diagnosis of heterozygotes
for acute intermittent porphyria were established.
Related Results
Yeast Porphobilinogen Deaminase also
Forms Enzyme-Pyrrole Intermediates
Yeast Porphobilinogen Deaminase also
Forms Enzyme-Pyrrole Intermediates
The enzyme porphobilinogen deaminase (PBG deaminase. EC 4.3.1.8) catalyzes
the condensation of four molecules of PBG to give the linear tetrapyrrol, hydroxymethylbilane.
It has bee...
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