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Information on EC 4.2.1.33 - 3-isopropylmalate dehydratase
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EC Tree
4.2.1.33 3-isopropylmalate dehydrataseIUBMB Comments
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.
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Word Map
- 4.2.1.33
- aconitase
-
4.3.1.2
- homoaconitase
-
mesaconic
-
2s,3s-3-methylaspartic
- citramalate
-
bcaas
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tetanomorphum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
isopropylmalate isomerase, leucd, alpha-isopropylmalate isomerase, isopropylmalate dehydratase, ipm isomerase, mj0499, alpha-ipm isomerase, leu1s, ipmi ssu1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alpha-IPM isomerase
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alpha-isopropylmalate isomerase
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beta-Isopropylmalate dehydratase
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dehydratase,beta-isopropylmalate
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IPM dehydratase
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IPMI
isopropylmalate dehydratase
isopropylmalate isomerase
leuC
LeuCD
MJ0499
SOI10
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Superoxide-inducible protein 10
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additional information
IPMI
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isopropylmalate isomerase
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isopropylmalate isomerase
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MJ0499
gene name, large subunit of 3-isopropylmalate dehydratase
MJ0499
gene name, large subunit of 3-isopropylmalate dehydratase
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additional information
the enzyme belongs to the aconitase superfamily
additional information
the enzyme belongs to the aconitase superfamily
additional information
the enzyme belongs to the aconitase superfamily
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additional information
the enzyme belongs to the aconitase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
overall reaction
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2-isopropylmaleate + H2O = (2S)-2-isopropylmalate
(1b)
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(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
(1a)
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(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
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(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
mechanism, equilibrium in vitro favors reaction opposite the direction of leucine biosynthesis
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(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
equilibrium concentration ratios
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(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
feedback regulation by leucine
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(2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
transcriptional feedback regulation by leucine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)
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.
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CAS REGISTRY NUMBER
COMMENTARY
37290-72-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
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?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
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?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
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-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
isomerization via a dehydration and a hydration step
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?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
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?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
isomerization via a dehydration and a hydration step
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?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
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?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
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?
2-isopropylmaleate + H2O
3-isopropylmalate
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2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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2-isopropylmaleate + H2O
?
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high activities in leu-1 mutants which have accumulated great amounts of inducer
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2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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3-isopropylmalate
2-isopropylmaleate + H2O
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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NMR and mass spectrometric compound determination and analysis, overview
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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citrate, aconitate, isocitrate are not substrates
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additional information
?
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citrate, aconitate, isocitrate are not substrates
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate
(2S)-2-isopropylmalate
O59393
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
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?
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
Q58673
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?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
Q94AR8 AND Q9ZW84, Q94AR8, Q9LYT7, Q9ZW84, Q9ZW85
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?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
Q94AR8 AND Q9ZW84
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?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
P9WK95, P9WQF5
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?
(2S)-2-isopropylmalate + H2O
(2R,3S)-3-isopropylmalate
P9WK95, P9WQF5
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-
?
2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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-
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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
-
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-
2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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2-isopropylmaleate + H2O
?
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second of three reactions of leucine biosynthesis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
the structure of the protein has unbound Fe-S clusters and contains a fourth cysteine in the active site
additional information
additional information
-
no requirement
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
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recovery after restoration of lower ionic strength shows hysteresis effect
beta-carboxy-beta-hydroxyisocaproate
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synthetic, racemic mixture
KCN
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complete inactivation at 10 mM; inactivation prevented by ammonium sulfate
mercaptoethanol
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protection by substrate
sulfhydryl compounds
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protection by substrate
additional information
-
inhibition at pH 4.5-5.0, reactivation at neutral pH
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additional information
-
additional compounds tested, without effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no requirement
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity with citraconate 4.8-fold and 7.4-fold higher than with standard substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6 - 8
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at pH 6.0, 20% of optimum activity, activity varies only about 20% between pH 7.0 and 8.0
6 - 8
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at pH 6.0, 20% of optimum activity, activity varies only about 20% between pH 7.0 and 8.0
6 - 8
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at pH 6.0, 20% of optimum activity, activity varies only about 20% between pH 7.0 and 8.0
6 - 8
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at pH 6.0, 20% of optimum activity, activity varies only about 20% between pH 7.0 and 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large subunit of 3-isopropylmalate dehydratase
SwissProt
brenda
the Arabidopsis genome encodes one potential large subunit and three potential small subunits, encoded by AtleuC and AtleuD genes
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brenda
large subunit of 3-isopropylmalate dehydratase
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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expression in all floral tissues including sepal, stamen, pistil as well as pollen grains, but it is only present at both ends of developing siliques
brenda
additional information
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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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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analysis of subcellular localization of AtLeuC and AtLeuDs within Arabidopsis chloroplast compartments, overview
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brenda
; presence of different heterodimeric IPMIs in chloroplasts with distinct substrate specificities for Leu or glucosinolate metabolism; presence of different heterodimeric IPMIs in chloroplasts with distinct substrate specificities for Leu or glucosinolate metabolism; presence of different heterodimeric IPMIs in chloroplasts with distinct substrate specificities for Leu or glucosinolate metabolism; 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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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); 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; 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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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
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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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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
-
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
-
physiological function
an intact IPMI small subunit 1 gene seems to be crucial for the development of mature viable seeds; 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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
additional information
-
complementation pair enzymes have higher molecular weights of 169000-185000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
monomer
additional information
heterodimer
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and 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
heterodimer
-
IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and 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
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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
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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
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol monomethyl ether 2000 and 0.1 MTris-HCl (pH 7.9)
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G456D
additional information
G456D
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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
G456D
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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
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additional information
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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
additional information
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construction of three C-terminally truncated variants of small subunit LeuD
additional information
construction of three C-terminally truncated variants of small subunit LeuD
additional information
construction of three C-terminally truncated variants of small subunit LeuD
additional information
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construction of three C-terminally truncated variants of small subunit LeuD
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
additional information
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very heat sensitive, high ionic strenght stabilizes enzyme against heat inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
half-life 2-3 h in potassium phosphate buffer, ph 6.8., 0-5°C, beta-isopropylmalate at 1 mM increases half-life to 15 h
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loss of activity after repeated freezing and thawing
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
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substrate stabilizes
unstable in phosphate buffer at pH 7.0, 10% loss of activity per h at 0°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
nickel-affinity column chromatography and Superdex 200 gel filtration
variants LeuD-1-156 and LeuD-1-168, by centrifugation, on Ni-NTA column and by gel filtration, more than 95% pure
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of FLAG-tagged LeuC and of the three LeuD isoforms in transgenic Arabidosis thaliana plants, interaction analysis, overview
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expression of His6-tagged LeuD in Escherichia coli strain BL21(DE3)
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; recombinant expression of GFP-tagged large and small subunit 1 in Arabidopsis thaliana leaves
variants LeuD-1-156 and LeuD-1-168, ligated into the pETM-11 expression vector, expressed in Escherichia coli BL21(DE3) RP
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in ipmi ssu2-1 plants, absence of mature mRNAs in homozygous plants and the knockout of these genes by T-DNAs; in ipmi ssu3-1 plants, absence of mature mRNAs in homozygous plants and the knockout of these genes by T-DNAs; 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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Arabidopsis thaliana (Q94AR8 AND Q9ZW84), Arabidopsis thaliana (Q94AR8), Arabidopsis thaliana (Q9LYT7), Arabidopsis thaliana (Q9ZW84), Arabidopsis thaliana (Q9ZW85), 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, Mycobacterium tuberculosis (P9WK95), Mycobacterium tuberculosis (P9WQF5), 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, Methanocaldococcus jannaschii (P81291), 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, Methanocaldococcus jannaschii (Q58673)
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
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