The enzyme, characterized from the plant Arabidopsis thaliana, is involved in the L-methionine side-chain elongation pathway, forming substrates for the biosynthesis of aliphatic glucosinolates. By catalysing a dehydration of a 2-[(ω-methylsulfanyl)alkyl]maleate, followed by a hydration at a different position, the enzyme achieves the isomerization of its substrates. The enzyme is a heterodimer comprising a large and a small subunits. The large subunit can also bind to an alternative small subunit, forming EC 4.2.1.33, 3-isopropylmalate dehydratase, which participates in L-leucine biosynthesis.
The expected taxonomic range for this enzyme is: Arabidopsis thaliana
The enzyme, characterized from the plant Arabidopsis thaliana, is involved in the L-methionine side-chain elongation pathway, forming substrates for the biosynthesis of aliphatic glucosinolates. By catalysing a dehydration of a 2-[(omega-methylsulfanyl)alkyl]maleate, followed by a hydration at a different position, the enzyme achieves the isomerization of its substrates. The enzyme is a heterodimer comprising a large and a small subunits. The large subunit can also bind to an alternative small subunit, forming EC 4.2.1.33, 3-isopropylmalate dehydratase, which participates in L-leucine biosynthesis.
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
Substrates: the enzyme catalyzes a two-step reaction via a dehydration of 2-(2-methylthio)ethylmalate and a hydration resulting in an isomerization at position 2/3 to form 3-(2-methylthio)ethylmalate Products: -
isopropylmalate isomerase (IPMI) large subunit mutants reveal accumulation of intermediates of both Leu biosynthesis and Met chain elongation, and an altered composition of aliphatic glucosinolates demonstrating the function of this gene in both pathways In contrast, the small subunits appear to be specialized to either Leu biosynthesis, EC 4.2.1.133, or Met chain elongation, EC 4.2.1.170, metabolic profiling, overview
isopropylmalate isomerase (IPMI) large subunit mutants reveal accumulation of intermediates of both Leu biosynthesis and Met chain elongation, and an altered composition of aliphatic glucosinolates demonstrating the function of this gene in both pathways In contrast, the small subunits appear to be specialized to either Leu biosynthesis, EC 4.2.1.133, or Met chain elongation, EC 4.2.1.170, metabolic profiling, overview
the enzyme is involved in methine elongation and in glucosinolate core biosynthesis and side-chain modification. IPMI small subunits are imported into the chloroplast, the localization of the Met chain elongation pathway in these organelles. The large IPMI subunit is involved in both Leu and glucosinolate metabolism, while the small subunits appear to be specific for each pathway. The small subunits IPMI SSU2 and IPMI SSU3 function in Met chain elongation
the enzyme is involved in methine elongation and in glucosinolate core biosynthesis and side-chain modification. IPMI small subunits are imported into the chloroplast, the localization of the Met chain elongation pathway in these organelles. The large IPMI subunit is involved in both Leu and glucosinolate metabolism, while the small subunits appear to be specific for each pathway. The small subunits IPMI SSU2 and IPMI SSU3 function in Met chain elongation
Knill, T.; Reichelt, M.; Paetz, C.; Gershenzon, J.; Binder, S.
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation
Plant Mol. Biol.
71
227-239
2009
Arabidopsis thaliana (Q94AR8 AND Q9LYT7), Arabidopsis thaliana (Q94AR8 AND Q9ZW85), Arabidopsis thaliana Col-0 (Q94AR8 AND Q9LYT7), Arabidopsis thaliana Col-0 (Q94AR8 AND Q9ZW85)
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