Results 121 to 130 of about 5,001 (177)
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Interaction of analogues of porphobilinogen with porphobilinogen deaminase
Journal of the Chemical Society, Perkin Transactions 1, 19962-Methylporphobilinogen 5 and 8,9-didehydroporphobilinogen 7 are only weak inhibitors of porphobilinogen deaminase (hydroxymethylbilane synthase). The phosphonate analogue 8 and 9-fluoroporphobilinogen 9 are good inhibitors, however, and also act as slow substrates (the first unnatural substrates known for this enzyme).
Finian J. Leeper, Martin Rock
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Nature, 1955
Chemical Synthesis of Porphobilinogen: Synthesis of Porphobilinogen and iso-Porphobilinogen Carboxylic ...
K. S. N. PRASAD, R. RAPER
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Chemical Synthesis of Porphobilinogen: Synthesis of Porphobilinogen and iso-Porphobilinogen Carboxylic ...
K. S. N. PRASAD, R. RAPER
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Nature, 1955
Chemical Synthesis of Porphobilinogen: Decarboxylation of Porphobilinogen- and iso-Porphobilinogen-α-Carboxylic ...
C. RIMINGTON, S. KROL
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Chemical Synthesis of Porphobilinogen: Decarboxylation of Porphobilinogen- and iso-Porphobilinogen-α-Carboxylic ...
C. RIMINGTON, S. KROL
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The porphobilinogen synthase family of metalloenzymes
Acta Crystallographica Section D: Biological Crystallography, 2000The porphobilinogen synthase (PBGS) family of enzymes catalyzes the first common step in the biosynthesis of the essential tetrapyrroles such as chlorophyll and porphyrin. Although PBGSs are highly conserved at all four levels of protein structure, there is considerable diversity in the use of divalent cations for the catalytically essential and ...
Eileen K Jaffe
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Canadian Journal of Chemistry, 1957
The pyrrole Ib has been converted by several routes into 5-carboxy-porphobilinogen (IIe), the lactam of which is easily decarboxylated to porphobilinogen lactam (IVc). Hydrolysis of the latter gives porphobilinogen (V).
A. H. Jackson, S. F. MacDonald
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The pyrrole Ib has been converted by several routes into 5-carboxy-porphobilinogen (IIe), the lactam of which is easily decarboxylated to porphobilinogen lactam (IVc). Hydrolysis of the latter gives porphobilinogen (V).
A. H. Jackson, S. F. MacDonald
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Nature, 1953
WE recently described a number of reactions of porphobilinogen, from which we concluded that it has the structure (I); but it was not then possible to eliminate the alternative structure in which the positions of the two β-substituents are reversed1.
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WE recently described a number of reactions of porphobilinogen, from which we concluded that it has the structure (I); but it was not then possible to eliminate the alternative structure in which the positions of the two β-substituents are reversed1.
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The enzymatic inactivation of porphobilinogen deaminase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract 1. 1. Porphobilinogen deaminase was inhibited by pyrrolooxygenase, a mixed-function oxidase which inhibits tryptophan-containing enzymes in the presence of sodium dithionite. 2. 2. Both enzymes were isolated from wheat germ but it was found that pyrrolooxygenase acted on deaminases from different origins. 3. 3.
R B, Frydman, B, Frydman
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Reliability of the porphobilinogen screening assay
Pathology, 1990A survey conducted by the Australian Association of Clinical Biochemists Porphyrin Working Party on urinary porphobilinogen screening showed good sensitivity (75-97.5%). This is contrary to reports in the literature and to our own observations. We therefore assessed a widely used screening method (Watson-Schwartz) and found poor sensitivity (40-69 ...
J E, Buttery, A M, Carrera, P R, Pannall
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