Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled
the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled
the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid
semi-quantitative RT-PCR analysis of temporal and spatial expression of AtLeuC and AtLeuD genes, overview. The tissue-specifis expression analysis reveals that the patterns of small subunits AtLeuD1 and AtLeuD2 expression are similar, but distinct from that of AtLeuD3
presence of different heterodimeric IPMIs in chloroplasts with distinct substrate specificities for Leu or glucosinolate metabolism. Import of the IPMI small subunit 2:GFP fusion protein into chloroplasts
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
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
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
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
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
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
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
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
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
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
the small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview. Presence of two LeuD subfamilies, structure modeling, overview
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview. Presence of two LeuD subfamilies, structure modeling, overview
sitting-drop vapour-diffusion methodand hanging-drop vapour diffusion at 20°C, structures of oxidized and reduced forms of the large subunit of isopropylmalate isomerase (ox-MJ0499 and red-MJ0499, respectively) are reported at 1.8 and 2.7 A resolution, respectively. Significant large conformational changes are observed in the active site of red-MJ0499 when compared with ox-MJ0499
small subunit LeuD variants, X-ray diffraction structure determination and analysis at resolutions of 2.0 A for LeuD_1-156, 1.2 A for LeuD_1-168, and 2.5 A for LeuD_1-186, respectively
variants LeuD-1-156 and LeuD-1-168, by sitting-drop vapour-diffusion method, crystals of LeuD-1-156 belong to the hexagonal system (space group P6122 or P6522) with up to four subunits in the asymmetric unit, whereas the crystals of LeuD-1-168 belong to the monoclinic system (space group P21) with two subunits in the asymmetric unit. Both crystals diffract to beyond 2.0 A resolution
crystal structure isopropylmalate isomerase small subunit. Four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. The structure reveals the formation of intermolecular disulfide linkages, and it provides insight into the dual substrate specificity of the enzyme
mutation in the 3-isopropylmalate dehydratase large subunit gene (leuC). Introduction of the leuC mutation into a defined L-lysine producer, AHD-2 (hom59 and lysC311), by allelic replacement leads to the phenotype of a partial requirement for L-leucine and approximately 14% increased L-lysine production
mutation in the 3-isopropylmalate dehydratase large subunit gene (leuC). Introduction of the leuC mutation into a defined L-lysine producer, AHD-2 (hom59 and lysC311), by allelic replacement leads to the phenotype of a partial requirement for L-leucine and approximately 14% increased L-lysine production
construction of AtLeuD1 T-DNA knockout mutant and AtLeuD -RNAi plants, i.e. specific AtLeuD2 -RNAi, AtLeuD -RNAi, atleud1 /AtLeuD2 -RNAi and atleud1 /AtLeuD -RNAi. Lethal phenotype of the atleud3 mutant
stabilized by high concentrations of glycerol and ammonium sulfate which also inhibit activity, half-life with 50% glycerol, 2.07 M ammonium sulfate, and 30% glycerol plus 830 mM ammonium sulfate: 50 h, 57 h, and 90 h, respectively, instead of 2-3 h without, stabilization probably due to changes in intramolecular interactions
full length reading frame of IPMI small subunit 2 fused in frame to the 5' end of the gene encoding the green fluorescent protein in the vector psmGFP4. Construct transiently expressed in tobacco protoplasts and stably transformed into Arabidopsis plants
in the ipmilsu1-2mutant mRNA levels are reduced to 65 and 50% of the wild-type standard in seedlings and rosette leaves, respectively, while IPMI large subunit 1 transcript levels are reduced to 40 and 27% of wild-type in these tissues of ipmi lsu1-1 plants. Strongest reduction in ipmi lsu1-3 seedlings (21% of wild-type), while the IPMI large subunit 1 mRNA level in ipmi lsu1-3 reaches about 29% of the wild-type level in leaves
Karuppasamy, M.; Geerlof, A.; Schuldt, L.; Mueller-Dieckmann, C.; Weiss, M.S.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the small subunit of isopropylmalate isomerase (Rv2987c) from Mycobacterium tuberculosis
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
Yasutake, Y.; Yao, M.; Sakai, N.; Kirita, T.; Tanaka, I.
Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme
Imhof, J.; Huber, F.; Reichelt, M.; Gershenzon, J.; Wiegreffe, C.; Laechler, K.; Binder, S.
The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation