Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
overall reaction
-
-
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
2-isopropylmaleate + H2O = (2S)-2-isopropylmalate
(1b)
-
-
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
stoichiometry of reaction, enzyme also hydrates 2-isopropylmaleate to 3-hydroxy-4-methyl-3-carboxypentanoate, interconversion between the 2 isomers
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
equilibrium concentration ratios
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
feedback regulation by leucine
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
mechanism, equilibrium in vitro favors reaction opposite the direction of leucine biosynthesis
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
transcriptional feedback regulation by leucine
-
(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
(1a)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3S)-3-isopropylmalate
(2S)-2-isopropylmalate
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
-
-
?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
3-isopropylmalate
2-isopropylmaleate + H2O
?
3-isopropylmalate
2-isopropylmaleate + H2O
alpha-hydroxy-beta-carboxyisocaproate
?
-
-
-
-
?
beta-carboxy-beta-hydroxyisocaproate
?
additional information
?
-
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
-
?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
isomerization via a dehydration and a hydration step
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
isomerization via a dehydration and a hydration step
-
-
?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
high activities in leu-1 mutants which have accumulated great amounts of inducer
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
beta-carboxy-beta-hydroxyisocaproate
?
-
-
-
-
?
beta-carboxy-beta-hydroxyisocaproate
?
-
-
-
-
?
citraconate
?
-
-
-
-
?
dimethylcitraconate
?
-
-
-
-
?
dimethylcitraconate
?
-
-
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
NMR and mass spectrometric compound determination and analysis, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
citrate, aconitate, isocitrate are not substrates
-
-
?
additional information
?
-
-
citrate, aconitate, isocitrate are not substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3S)-3-isopropylmalate
(2S)-2-isopropylmalate
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
-
-
?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
-
?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
-
-
-
?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
-
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
high activities in leu-1 mutants which have accumulated great amounts of inducer
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
2-isopropylmaleate + H2O
?
-
second of three reactions of leucine biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
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
-
lethal phenotype of the atleud3 mutant with a defect in female gametophyte development
malfunction
-
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
-
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
-
metabolism
-
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
-
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
-
physiological function
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
-
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
-
the small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation
additional information
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 46000 + x * 18000, SDS-PAGE
multimer
-
active as monomer, can aggregate to dimers or multimers in cell
tetramer
-
trimer or tetramer of 2 different polypeptide subunits
trimer
-
trimer or tetramer of 2 different polypeptide subunits
heterodimer
-
heterodimer
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview
heterodimer
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
heterodimer
-
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
-
heterodimer
-
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview
-
monomer
-
variants LeuD-1-156 and LeuD-1-168, gel-filtration
monomer
-
variants LeuD-1-156 and LeuD-1-168, gel-filtration
-
monomer
-
1*90000, SDS-PAGE
additional information
structure and oligomeric state of Mtb-LeuD in the crystal structure, overview
additional information
structure and oligomeric state of Mtb-LeuD in the crystal structure, overview
additional information
-
structure and oligomeric state of Mtb-LeuD in the crystal structure, overview
additional information
-
structure and oligomeric state of Mtb-LeuD in the crystal structure, overview
-
additional information
-
amino acid analysis, protein contains hinge regions that are very sensitive to proteolytic attack
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gross, S.R.
Isopropylmalate isomerase (Neurospora)
Methods Enzymol.
17A
786-790
1970
Neurospora sp., Salmonella sp.
-
brenda
Bigelis, R.; Umbarger, H.E.
Yeast alpha-isopropylmalate isomerase. Factors affecting enzyme stability and enzyme activity
J. Biol. Chem.
251
3545-3552
1976
Saccharomyces cerevisiae
brenda
Reichenbecher Jr, V.E.; Gross, S.R.
Structural features of normal and complemented forms of the Neurospora isopropylmalate isomerase
J. Bacteriol.
133
802-810
1978
Neurospora crassa
brenda
Gross, S.R.; Umbarger, H.E.
The biosynthesis of leucine: II. The enzymic isomerization of beta-carboxy-beta-hydroxyisocaproate and alpha-hydroxy-beta-carboxyisocaproate
Biochemistry
2
1046-1052
1963
Neurospora crassa, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Reichenbecher, V.E.; Fischer, M.; Gross, S.R.
Regulation of isopropylmalate synthesis in Neurospora crassa
J. Bacteriol.
133
794-801
1978
Neurospora crassa
brenda
Kohlhaw, G.B.
Isopropylmalate dehydratase from yeast
Methods Enzymol.
166
423-429
1988
Saccharomyces cerevisiae
brenda
Bode, R.; Birnbaum, D.
Some properties of the leucine-biosynthesizing enzymes from Candida maltosa
J. Basic Microbiol.
31
21-26
1991
Candida maltosa
-
brenda
Hayashi, M.; Mizoguchi, H.; Ohnishi, J.; Mitsuhashi, S.; Yonetani, Y.; Hashimoto, S.; Ikeda, M.
A leuC mutation leading to increased L-lysine production and rel-independent global expression changes in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
72
783-789
2006
Corynebacterium glutamicum, Corynebacterium glutamicum B-6
brenda
Hamaji, T.; Ferris, P.J.; Coleman, A.W.; Waffenschmidt, S.; Takahashi, F.; Nishii, I.; Nozaki, H.
Identification of the minus-dominance gene ortholog in the mating-type locus of Gonium pectorale
Genetics
178
283-294
2008
Gonium pectorale
brenda
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
Acta Crystallogr. Sect. F
65
136-139
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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), Arabidopsis thaliana (Q94AR8 AND Q9ZW84), Arabidopsis thaliana (Q9LYT7), Arabidopsis thaliana (Q9ZW84), Arabidopsis thaliana (Q9ZW85), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q94AR8 AND Q9ZW84)
brenda
He, Y.; Chen, B.; Pang, Q.; Strul, J.M.; Chen, S.
Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis
Plant Cell Physiol.
51
1480-1487
2010
Arabidopsis thaliana
brenda
Manikandan, K.; Geerlof, A.; Zozulya, A.V.; Svergun, D.I.; Weiss, M.S.
Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis
Proteins
79
35-49
2011
Mycobacterium tuberculosis (P9WK95), Mycobacterium tuberculosis (P9WQF5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WK95), Mycobacterium tuberculosis H37Rv (P9WQF5)
brenda
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
J. Mol. Biol.
344
325-333
2004
Pyrococcus horikoshii (O59393), Pyrococcus horikoshii
brenda
Lee, E.H.; Lee, K.; Hwang, K.Y.
Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii
Acta Crystallogr. Sect. D
70
922-931
2014
Methanocaldococcus jannaschii (P81291), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (P81291)
brenda
Lee, E.H.; Cho, Y.W.; Hwang, K.Y.
Crystal structure of LeuD from Methanococcus jannaschii
Biochem. Biophys. Res. Commun.
419
160-164
2012
Methanocaldococcus jannaschii (Q58673), Methanocaldococcus jannaschii
brenda
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
PLoS ONE
9
e91071
2014
Arabidopsis thaliana
brenda
Chen, L.Q.; Chhajed, S.; Zhang, T.; Collins, J.M.; Pang, Q.; Song, W.; He, Y.; Chen, S.
Protein complex formation in methionine chain-elongation and leucine biosynthesis
Sci. Rep.
11
3524
2021
Arabidopsis thaliana, Arabidopsis thaliana Col0
brenda