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5 resultats
Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase.
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The structure of a phenylalanine aminomutase (TcPAM) from Taxus canadensis has been determined at 2.4 Å resolution. The active site of the TcPAM contains the signature 4-methylidene-1H-imidazol-5(4H)-one prosthesis, observed in all catalysts of the class I lyase-like family. This catalyst isomerizes
CYP79 P450 monooxygenases in gymnosperms: CYP79A118 is associated with the formation of taxiphyllin in Taxus baccata.
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Conifers contain P450 enzymes from the CYP79 family that are involved in cyanogenic glycoside biosynthesis. Cyanogenic glycosides are secondary plant compounds that are widespread in the plant kingdom. Their biosynthesis starts with the conversion of aromatic or aliphatic amino acids into
A Tyrosine Aminomutase from Rice (Oryza sativa) Isomerizes (S)-α- to (R)-β-Tyrosine with Unique High Enantioselectivity and Retention of Configuration.
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A recently discovered 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO)-dependent tyrosine aminomutase (OsTAM) from rice [Yan, J., et al. (2015) Plant Cell 27, 1265] converts (S)-α-tyrosine to a mixture of (R)- and (S)-β-tyrosines, with high (94%) enantiomeric excess, which does not change with pH,
Stereochemical aspects of the biosynthesis of the epimeric cyanogenic glucosides dhurrin and taxiphyllin.
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Dhurrin, I ((S)-p-hydroxymandelonitrile-beta-D-glucopyranoside), and taxiphyllin, II (the (R) epimer), occur in the genera Sorghum and Taxus, respectively. Both derive biosynthetically from L-tyrosine via the hydroxylation of p-hydroxyphenylacetonitrile, III. (3R)- and (3S)-L-[3-3H1]tyrosine,
Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis.
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Biosynthesis of the N-benzoyl phenylisoserinoyl side chain of the anticancer drug Taxol starts with the conversion of 2S-alpha-phenylalanine to 3R-beta-phenylalanine by phenylalanine aminomutase (PAM). A gene cloning approach was based on the assumption that PAM would resemble the well known plant
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