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It is well known that phenylpropanoid biosynthesis is a very complex process and that multiple enzyme metabolites are produced.
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More challenging still, it remains to be seen whether we can alter age-related changes in metabolite correlations by feeding two or more metabolites to flies simultaneously, or altering expression patterns of multiple enzymes associated with metabolites whose correlations change with age.
The modulation but not rescue of metformin toxicity by salvage metabolites strongly suggests that metformin's antifolate activity does not likely involve the direct inhibition of multiple enzyme targets in both purine and pyrimidine synthesis.
One additional source of information is protein structure, which we, and others, have used successfully to predict the substrates of enzymes, including multiple enzymes forming a pathway by metabolite docking.
This CRISPRi-guided balancing of expression of MVA pathway genes led to enhanced production of -α-bisabolol (C15) and lycopene (C40) and alleviation of cell growth inhibition that may be caused by expression of multiple enzymes or production of toxic intermediate metabolites in the MVA pathway.
The difficulties for generalizing predictions are potentiated by the fact that in almost all cases, multiple enzymes with differing affinities to their substrates (be they the starting material or toxic metabolites) are involved in the toxication and in the detoxication of a given toxic species.
The formation of specialized metabolites enables plants to respond to biotic and abiotic stresses, but requires the sequential action of multiple enzymes.
Methotrexate inhibits multiple enzymes beyond dihydrofolate reductase.
The cytoplasm of bacteria contains high concentrations of enzymes, metabolites, and salts.
Considering the 15 enzyme-metabolite pairs for which the metabolite was either the direct substrate or the direct product of the enzyme, few significant correlations were found.
These are major enzymes catalyzing β-nicotinamide adenine dinucleotide phosphate (NADPH) dependent oxidative metabolism of estrogen to multiple hydroxylated metabolites.
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CEO of Professional Science Editing for Scientists @ prosciediting.com