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- Abel, S. (1)
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Kopycki, J.; Wieduwild, E.; Kohlschmidt, J.; Brandt, W.; Stepanova, A.N.; Alonso, J.M.; Pedras, M.S.; Abel, S.; Grubb, C.D. Kinetic analysis of Arabidopsis glucosyltransferase UGT74B1 illustrates a general mechanism by which enzymes can escape product inhibition Biochem J 450, 37-46, (2013) DOI: 10.1042/BJ20121403
Plant genomes
encode numerous small molecule glycosyltransferases which modulate the
solubility, activity, immunogenicity and/or reactivity of hormones,
xenobiotics and natural products. The products of these enzymes can
accumulate to very high concentrations, yet somehow avoid inhibiting
their own biosynthesis. Glucosyltransferase UGT74B1
(UDP-glycosyltransferase 74B1) catalyses the penultimate step in the
core biosynthetic pathway of glucosinolates, a group of natural products
with important functions in plant defence against pests and pathogens.
We found that mutation of the highly conserved Ser284 to leucine [wei9-1
(weak ethylene insensitive)] caused only very mild morphological and
metabolic phenotypes, in dramatic contrast with knockout mutants,
indicating that steady state glucosinolate levels are actively regulated
even in unchallenged plants. Analysis of the effects of the mutation
via a structural modelling approach indicated that the affected serine
interacts directly with UDP-glucose, but also predicted alterations in
acceptor substrate affinity and the kcat value, sparking an interest in
the kinetic behaviour of the wild-type enzyme. Initial velocity and
inhibition studies revealed that UGT74B1 is not inhibited by its
glycoside product. Together with the effects of the missense mutation,
these findings are most consistent with a partial rapid equilibrium
ordered mechanism. This model explains the lack of product inhibition
observed both in vitro and in vivo, illustrating a general mechanism
whereby enzymes can continue to function even at very high
product/precursor ratios.
Feussner, I.; Fritz, I.G.; Hause, B.; Ullrich, W.R.; Wasternack, C. Induction of a new lipoxygenase form in cucumber leaves by salicylic acid or 2,6-dichloroisonicotinic acid Bot. Acta 110, 101-108, (1997) DOI: 10.1111/j.1438-8677.1997.tb00616.x
Changes in lipoxygenase (LOX) protein pattern and/or activity were investigated in relation to acquired resistance of cucumber (Cucumis sativus L.) leaves against two powdery mildews, Sphaerotheca fuliginea (Schlecht) Salmon and Erysiphe cichoracearum DC et Merat. Acquired resistance was established by spraying leaves with salicylic acid (SA) or 2,6-dichloroisonicotinic acid (INA) and estimated in whole plants by infested leaf area compared to control plants. SA was more effective than INA. According to Western blots, untreated cucumber leaves contained a 97 kDa LOX form, which remained unchanged for up to 48 h after pathogen inoculation. Upon treatment with SA alone for 24 h or with INA plus pathogen, an additional 95 kDa LOX form appeared which had an isoelectric point in the alkaline range. For the induction of this form, a threshold concentration of 1 mM SA was required, higher SA concentrations did not change LOX-95 expression which remained similar between 24 h and 96 h but further increased upon mildew inoculation. Phloem exudates contained only the LOX-97 form, in intercellular washing fluid no LOX was detected. dichloroisonicotinic localization revealed LOX protein in the cytosol of the mesophyll cells without differences between the forms.