By Alton Meister

ISBN-10: 047012301X

ISBN-13: 9780470123010

ISBN-10: 0471868604

ISBN-13: 9780471868606

A continuous authoritative sequence reviewing study into enzymology and comparable parts of molecular biology. offers six papers by means of major specialists.

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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 55

Sample text

The enzymes were distinguished by differences in stability upon storage, gel chromatographic properties, changes in specific activity during the growth cycle, and substrate specificity. One enzyme, the Sadenosyl methionine :caffeic acid O-methyl transferase (CMT), catalyzed the formation of ferulic (XXVIII) and sinapic (XXIV) acids from caffeic (XXII) and 5-hydroxy ferulic acids, respectively (208). It had no activity against flavonoids or isoflavonoids, this being consistent with its role in the lignin pathway (208).

Rnax and P. vulguris enzymes by tetrathionate (181,183) argues against the involvement of essential SH groups for activity as suggested earlier (180). A mechanism for the isomerization reaction involving an acid-base catalyzed formation of a flav-3en4-01 intermediate followed by a stereospecific proton transfer to form the flavanone was proposed (179), and the possible involvement of an enzyme imidazole or amino group was suggested (181). More recently it was shown that the existence of the chalcone 2’-hydroxyl group in an ionized form was essential for activity (184), this requirement being observed in profiles for the variation of V,, with pH for the forward reaction catalyzed by the G.

Labeling experiments in CuC12- and ultraviolet light-treated seedlings of Medicugo sutivu have shown that neither 2',4'dihydroxy4-methoxy chalcone (XXXIII) nor dhdzein (XIX) is incorporated into medicarpin (IX), sativan (VI), or vestitol 0,whereas 2',4,4'-trihydroxychalcone (XXVI) and formononetin (XVI) are good precursors (148). These results confirm the requirement for a free chalcone (XXXIII) 0 4hydroxyl group in the enzyme-catalyzed reaction, and strongly suggest that methylation of this group is an integral part of the aryl migration process in M.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 55 by Alton Meister


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