For example, enzymes that prefer terephthalic acid (dicarboxylic acid) as the substrate and less so (or no activity at all) with benzoic acid (monocarboxylic acid).
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PETase and MHETase are two such enzymes.
A. PETase enzymes are known to prefer terephthalic acid, a dicarboxylic acid, as a substrate, while they exhibit significantly lower activity, or no activity at all, with benzoic acid, a monocarboxylic acid. PETase enzymes are a class of esterases that specifically catalyze the hydrolysis of polyethylene terephthalate (PET).
They are designed to recognize and interact with the terephthalic acid component of the PET molecule, the dicarboxylic acid portion. They are highly efficient in hydrolyzing PET and do not readily interact with or degrade monocarboxylic acids like benzoic acid.
B. MHETase is an enzyme involved in the degradation of mono-(2-hydroxyethyl) terephthalate (MHET), a product of PET breakdown. It has a high affinity for dicarboxylic acids, like terephthalic acid, and prefers to cleave the ester bond at the dicarboxylic end of MHET. This enzyme exhibits very low or no activity towards monocarboxylic acids, like benzoic acid as it cannot properly bind or cleave the ester bond at the monocarboxylic end.
You may want to refer to the article attached below for more information.
Article Biodegradation of polyethylene and polystyrene: From microbi...
Best,
The TCA cycle intermediates alpha-ketoglutarate, succinate, fumarate malate and oxaloacetate all have 2 carboxylic acid groups, so the enzymes alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase and citrate synthase should prefer substrates with 2 carboxylic acid groups.
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