Substrates: enzyme catalyses the final step of (+)-carvone biosynthesis, which is developmentally regulated, key enzyme of the pathway is limonene-6-hydroxylase Products: -
Substrates: enzyme catalyses the final step of (+)-carvone biosynthesis, which is developmentally regulated, key enzyme of the pathway is limonene-6-hydroxylase Products: -
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
applicability of strains with high enzyme content or recombinant overproducing strains for production of (+)-carvone, which is used as a flavor compound
applicability of strains with high enzyme content or recombinant overproducing strains for production of (+)-carvone, which is used as a flavor compound
Bouwmeester, H.J.; Gershenzon, J.; Konings, M.C.J.M.; Croteau, R.
Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development
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