4.2.1.33: 3-isopropylmalate dehydratase
This is an abbreviated version!
For detailed information about 3-isopropylmalate dehydratase, go to the full flat file.
Reaction
Synonyms
3-isopropylmalate dehydratase, 3-isopropylmalate isomerase, Alpha-IPM isomerase, alpha-isopropylmalate isomerase, beta-Isopropylmalate dehydratase, dehydratase,beta-isopropylmalate, IPM dehydratase, IPM isomerase, IPMI, IPMI SSU1, isopropylmalate dehydratase, isopropylmalate isomerase, LEU1S, leuC, LeuCD, LeuD, MJ0499, More, SOI10, Superoxide-inducible protein 10
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General Information
General Information on EC 4.2.1.33 - 3-isopropylmalate dehydratase
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malfunction
metabolism
physiological function
additional information
for IPMI small subunit 1, no plants homozygous for the T-DNA allele can be obtained in either analyzed line (ipmi ssu1-1 or ipmi ssu1-2)
malfunction
homozygous ipmi 3-1mutants can be established. In leaves and seeds of the ipmi ssu3-1 mutant few significant changes in amino acid content. Met levels are unchanged in ipmi ssu3-1 and S-methylmethionine can not be detected
malfunction
homozygous ipmi ssu2-1 mutants can be established. Free amino acid content of the leaves and seeds of ipmi ssu2-1 plants is not substantially different from that of the wild-type. S-methylmethionine is not detectable in the ipmi ssu2-1 mutant. Profile of the methionine-derived glucosinolates in leaves of ipmi ssu2-1 does not show substantial variations from that of wild-type plants
malfunction
in leaves, ipmi lsu1-2 plants exhibit the weakest chemical phenotype in comparison to wild-type: transport or storage form of Met is barely detectable. Many more changes between the ipmi lsu1-1 and 1-3 plants and wild-type: accumulation of S-methylmethionine in rosette leaves of both mutants which is accompanied by 2fold increased levels of Met. Average 2-isopropylmalate content of 0.42 and 0.02 mg/g dry weight in leaves of ipmi lsu1-3 and ipmi lsu1-1 mutants, respectively, while this metabolite is undetectable in the ipmi lsu1-2 plants. Relative levels of 2-(3'-methylsulfinyl)propylmalate are 10/1/14 in ipmi lsu1-1, 1-2 and 1-3 plants
malfunction
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lethal phenotype of the atleud3 mutant with a defect in female gametophyte development
malfunction
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knockdown plants contain chloroplasts with abnormal morphology and show a severe macroscopic phenotype with narrow, often undulated leaves with yellow pale green leaf blades except at the vascular bundles, which show normal green color
malfunction
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. In large subunit single gene knockout mutant IPMI, the remaining IPMI LSU1 transcript is sufficient for some biosynthesis of Met-derived aliphatic glucosinolates and maintaining Leu levels comparable to wild-type plants
malfunction
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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. In large subunit single gene knockout mutant IPMI, the remaining IPMI LSU1 transcript is sufficient for some biosynthesis of Met-derived aliphatic glucosinolates and maintaining Leu levels comparable to wild-type plants
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isopropylmalate isomerase large subunit and small subunits form heterodimers to catalyze the isomerization of 2-isopropylmalate to 3-isopropylmalate in leucine biosynthesis in bacteria and archaea. Reverse genetics and metabolite profiling show that AtLeuD1 and AtLeuD2 function redundantly in aliphatic glucosinolate biosynthesis, but AtLeuD3 is not likely to be involved in this pathway
metabolism
the enzyme is involved in the leucine biosynthesis. The formation of leucine requires a three-step chain elongation, including a condensation of a 2-oxo acid with acetyl-CoA, an isomerization and an oxidation-decarboxylation, catalyzed by isopropylmalate synthase (IPMS), isopropylmalate isomerase (IPMI, also called a dehydratase) and isopropylmalate dehydrogenase (IPMDH), respectively. Leu biosynthesis is then completed by a transamination step catalyzed by a branched-chain aminotransferase that could be also involved in the formation of the other branched-chain amino acids. The large IPMI subunit is involved in both Leu and glucosinolate metabolism, while the small subunits appear to be specific for each pathway
metabolism
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the enzyme is involved in the leucine biosynthesis. The formation of leucine requires a three-step chain elongation, including a condensation of a 2-oxo acid with acetyl-CoA, an isomerization and an oxidation-decarboxylation, catalyzed by isopropylmalate synthase (IPMS), isopropylmalate isomerase (IPMI, also called a dehydratase) and isopropylmalate dehydrogenase (IPMDH), respectively. Leu biosynthesis is then completed by a transamination step catalyzed by a branched-chain aminotransferase that could be also involved in the formation of the other branched-chain amino acids. The large IPMI subunit is involved in both Leu and glucosinolate metabolism, while the small subunits appear to be specific for each pathway
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an intact IPMI small subunit 1 gene seems to be crucial for the development of mature viable seeds
physiological function
function of IPMI large subunit 1 in both the biosynthesis of Leu and in the Met chain elongation pathway of glucosinolate formation
physiological function
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isopropylmalate isomerase large subunit and small subunits form heterodimers to catalyze the isomerization of 2-isopropylmalate to 3-isopropylmalate in leucine biosynthesis in bacteria and archaea. AtLeuD3 plays an essential role in leucine biosynthesis and female gametophyte development
physiological function
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the small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation
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physical interaction between isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenases (IPMDHs) in planta. The complex formation may represent a new regulatory mechanism controlling Met chain-elongation and/or Leu biosynthesis
additional information
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physical interaction between isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenases (IPMDHs) in planta. The complex formation may represent a new regulatory mechanism controlling Met chain-elongation and/or Leu biosynthesis
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