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Biosynthesis of uroporphyrinogens. Interaction among 2-aminomethyltripyrranes and the enzymatic system.
TLDR
An outline of the most likely pathway of uroporphyrinogen III biosynthesis from porphobilinogen is given and the results obtained with 2-aminomethyldipyrrylmethanes are obtained. Expand
Biliverdin reductase: substrate specificity and kinetics.
TLDR
The substrate specificity of the different forms of rat liver biliverdin reductase was examined and it was found that they fitted a model of a moderate cooperative dimer where both ES and ES2 are catalytically active. Expand
The specificity of biliverdin reductase. A study with different biliverdin types.
TLDR
Results indicate that biliverdin reductase reduced bilitriene acids substituted with non-polar and polar residues to the bilirubins in the presence of NADPH. Expand
Biosynthesis of uroporphyrinogens from porphobilinogen: mechanism and the nature of the process.
TLDR
Different enzyme-bound dipyrrylmethanes are formed form the beginning of the process, and this can be demonstrated by using synthetic dipyrries and tripyrranes. Expand
Biosynthesis of uroporphyrinogens. Interaction among 2-(aminomethyl)bilanes and the enzymatic system.
TLDR
An outline of the most likely pathway of uroporphyrinogen III biosynthesis from porphobilinogen is given and results obtained with 2-aminomethyldipyrrylmethanes are obtained. Expand
The enzymatic incorporation of a dipyrrylmethane into uroporphyrinogen III
TLDR
It is proposed that both isomers originate by different pathways from the start of the polymerization and that the dipyrrylmethane 5 resulting from the formal head-to-head condensation of two units of porphobilinogen is a first intermediate of the enzymatic system involved in uroporphyrinogen polymerization. Expand
The enzymatic incorporation of a tripyrrane into uroporphyrinogen I
Porphyrins, chlorins and vitamin B12 share a common metabolic pathway through a long range of initial steps. Of crucial importance to this pathway is the biochemical mechanism involved in theExpand
The enantioselective participation of (S)- and (R)-diaminovaleric acids in the formation of delta-aminolevulinic acid in cyanobacteria.
TLDR
Glutamate 1-semialdehyde aminotransferase is highly but not absolutely enantioselective for (S)-4,5-diaminovaleric acid, and 4, 5-dioxovaleric Acid can function as amino acceptor not because of a physiological role in the C5 pathway of delta-aminolevulinic acid formation, but because of its structural resemblance to glutamate 1-Semialde Hyde. Expand
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