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Information on EC 1.1.1.41 - isocitrate dehydrogenase (NAD+) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P28241
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1.1.1.41 isocitrate dehydrogenase (NAD+)IUBMB Comments
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm . The enzyme from some species can also use NADP+ but much more slowly .
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tricarboxylic
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malic
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idh-mutant
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oncometabolite
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nadp+-dependent
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krebs
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codeletion
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preoperative
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radiotherapy
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lower-grade
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progression-free
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anaplastic
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high-grade
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gliomagenesis
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nadp-linked
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ten-eleven
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thoracis
- semitendinosus
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
isocitrate dehydrogenase, isocitrate dehydrogenase 2, isocitric dehydrogenase, nad-dependent isocitrate dehydrogenase, idh3a, nad-idh, nad-isocitrate dehydrogenase, nad-icdh, nad+-dependent isocitrate dehydrogenase, nad-linked isocitrate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-ketoglutaric-isocitric carboxylase
-
-
-
-
IDH1
isocitric acid dehydrogenase
-
-
-
-
isocitric dehydrogenase
-
-
-
-
NAD dependent isocitrate dehydrogenase
-
-
-
-
NAD isocitrate dehydrogenase
-
-
-
-
NAD isocitric dehydrogenase
-
-
-
-
NAD+-specific ICDH
-
-
-
-
NAD+-specific isocitrate dehydrogenase
NAD-linked isocitrate dehydrogenase
-
-
-
-
NAD-specific isocitrate dehydrogenase
-
-
-
-
IDH1
-
-
-
-
NAD+-specific isocitrate dehydrogenase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
reductive carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
isocitrate:NAD+ oxidoreductase (decarboxylating)
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [7]. The enzyme from some species can also use NADP+ but much more slowly [9].
CAS REGISTRY NUMBER
COMMENTARY
9001-58-5
-
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
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
additional information
?
-
-
allosteric regulation, enzyme specifically binds to 5'-untranslated regions of yeast mitochondrial mRNAs, and transcripts containing these regions allosterically inhibit the enzyme, which can be relieved by activator AMP in presence of isocitrate, complex formation, overview
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
catalytic residues binding isocitrate are located on subunit IDH2, while regulatory residues binding isocitrate are located on subunit IDH1
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
isocitrate binds at 2 functionally distinct sites
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme has a regulatory role in the tricarboxylic cycle
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation
-
-
?
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
additional information
?
-
-
allosteric regulation, enzyme specifically binds to 5'-untranslated regions of yeast mitochondrial mRNAs, and transcripts containing these regions allosterically inhibit the enzyme, which can be relieved by activator AMP in presence of isocitrate, complex formation, overview
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme has a regulatory role in the tricarboxylic cycle
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
dependent on, one NAD+ site per enzyme tetramer, two functional NAD+ binding sites in the wild-type enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
130-nucleotide transcript containing the 5'-untranslated regions of the yeast mitochondrial COX2 mRNA
-
inhibition with a 50% reduction in activity observed with 40 nM mRNA
-
beta-mercapto-alpha-ketoglutarate
-
inhibition in presence and absence of AMP, competitive inhibition
citrate
-
with constant concentrations of isocitrate, NAD+ and Mg2+ up to 10 mM and without AMP, citrate is an activator
D,L-hibiscusate
-
with constant concentrations of isocitrate, NAD+ and Mg2+ up to 10 mM and without AMP, D,L-hibiscusate is an activator
D,L-threo-alpha-methylisocitrate
-
inhibition in presence and absence of AMP, competitive inhibition
Fluorocitrate
-
with constant concentrations of isocitrate, NAD+ and Mg2+ up to 10 mM and without AMP, fluorocitrate is an activator
L-hibiscusate
-
with constant concentrations of isocitrate, NAD+ and Mg2+ up to 10 mM and without AMP, L-hibiscusate is an activator
L-malate
-
inhibition only in absence of AMP, competitive inhibition
mRNA
-
enzyme specifically binds to 5'-untranslated regions of yeast mitochondrial mRNAs, and transcripts containing these regions allosterically inhibit the enzyme, which can be relieved by activator AMP in presence of isocitrate, complex formation, overview
Diamide
-
treatment of the affinity-purified enzyme with diamide results in the formation of disulfide bonds and in decreased activity for the wild type enzyme, the effect is reversible by the addition of dithiothreitol
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
activation of the enzyme and reduction of enzyme inhibition by mitochondrial mRNA, highly enhanced by presence of isocitrate, complex formation, overview
AMP
-
allosteric activation, isocitrate binding is essential for binding of AMP to IDH1 subunits
DTT
-
decreases disulfide content of the enzyme, kinetics of enzyme mutants in presence or absence of DTT, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
D-isocitrate
-
octameric wild-type enzyme with AMP, without DTT, pH 7.4, 24°C
0.1
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S with AMP, with or without DTT, pH 7.4, 24°C
0.1
D-isocitrate
-
octameric wild-type enzyme with AMP and DTT, pH 7.4, 24°C
0.17
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP, without DTT, pH 7.4, 24°C
0.19
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP and DTT, pH 7.4, 24°C
0.2
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP and DTT, pH 7.4, 24°C
0.32
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP, without DTT, pH 7.4, 24°C
0.48
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C
0.5
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C
0.51
D-isocitrate
-
octameric wild-type enzyme without AMP, with DTT, pH 7.4, 24°C
0.53
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S without AMP and DTT, pH 7.4, 24°C
0.54
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S without AMP, with DTT, pH 7.4, 24°C
0.56
D-isocitrate
-
octameric wild-type enzyme without AMP and DTT, pH 7.4, 24°C
1.01
D-isocitrate
-
octameric enzyme mutant IDH1G15D/IDH2 without AMP and DTT, pH 7.4, 24°C
1.03
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S without AMP, with or without DTT, pH 7.4, 24°C
1.19
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C
1.3
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP, with DTT, pH 7.4, 24°C
1.6
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP and DTT, pH 7.4, 24°C
additional information
additional information
-
kinetics and ligand binding
-
additional information
additional information
-
kinetics and ligand binding
-
additional information
additional information
-
NAD+-specific D-isocitrate dehydrogenase is an allosterically regulated. AMP and NAD+ binding kinetics of enzyme mutants in presence or absence of DTT, overview
-
additional information
additional information
-
yeast NAD+-specific isocitrate dehydrogenase is an allosterically regulated
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
yeast IDH is regulated both by allostery and by covalent formation of a disulfide bond, and these regulatory mechanisms contribute to modulation of respiratory metabolism in vivo
additional information
additional information
-
interactions between sulfhydryl side chains of IDH2 Cys150 residues limit access to eight D-isocitrate and four AMP binding sites. In the presence of dithiothreitol, all ligand binding sites except for two potential NAD+ sites can be occupied
additional information
-
the IDH2 Cys-150 residue controls access to isocitrate binding sites. The wild-type enzyme displays four binding sites for isocitrate and two binding sites for AMP in the absence of dithiothreitol, and these numbers increase to eight and four in the presence of dithiothreitol, respectively
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
335000
37755
38000
38001
37755
4 * 38001, 4 * 37755, the enzyme consists of four IDH1 and four IDH2 subunits, the basic structural unit of the enzyme is an IDH1/IDH2 heterodimer
37755
-
4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation
38001
4 * 38001, 4 * 37755, the enzyme consists of four IDH1 and four IDH2 subunits, the basic structural unit of the enzyme is an IDH1/IDH2 heterodimer
38001
-
4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
additional information
octamer
-
alpha4beta4, IDH1 and IDH2, 4 * 38001 + 4 * 37755, SDS-PAGE
octamer
4 * 38001, 4 * 37755, the enzyme consists of four IDH1 and four IDH2 subunits, the basic structural unit of the enzyme is an IDH1/IDH2 heterodimer
octamer
-
the octameric enzyme is composed of four heterodimers of regulatory IDH1 and catalytic IDH2 subunits
octamer
-
4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation
octamer
-
the enzyme is composed of four heterodimers of a catalytic IDH2 subunit and a regulatory IDH1 subunit
additional information
-
model of binding sites for isocitrate of the 2 different subunits
additional information
-
subunit IDH2 contains catalytic isocitrate/Mg2+ and NAD+ binding sites whereas subunit IDH1 contains homologous binding sites, respectively, for cooperative binding of isocitrate and for allosteric binding of AMP. The subsunits share 42% sequence identity
additional information
-
the enzyme is composed of four heterodimers, in two heterotetramers, of a catalytic IDH2 subunit and a regulatory IDH1 subunit, IDH octamer structure, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I221A/V225A/V229A
mutant enzyme IDH1-IDH2(I221A/V225A/V229A) shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. Mutant enzyme IDH1-IDH2 (I221A/V225A/V229A) exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
V216A/S220A/V224A
IDH1(V216A/S220A/V224A)IDH2 mutant enzyme shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. IDH1(V216A/S220A/V224A)IDH2 mutant enzyme exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
V216A/S220A/V224A/I221A/V225A/V229A
in the absence of AMP, the IDH1(V216A/S220A/V224A)-IDH2(I221A/V225A/V229A) mutant enzyme demonstrates an about 30fold decrease in apparent Vmax relative to wild-type and a loss of cooperativity with respect to isocitrate and, in the presence of AMP, the apparent affinity of the enzyme for isocitrate is 35fold lower than that of the wild-type enzyme. This mutant enzyme also exhibits a significant decrease in apparent affinity for NAD+ (about 30fold in the absence of AMP and about 10fold in the presence of AMP relative to wild-type). The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme demonstrates decreases in apparent affnity for isocitrate of about 12fold in the absence of AMP and of about 26fold in the presence of AMP relative to wild-type. For this mutant enzyme, with respect to isocitrate, allosteric activation by AMP and cooperativity in the absence of AMP are no longer apparen. The mutant enzyme is not fully functional in vivo
A108R/F136Y/T241D/N245D
-
site-directed mutagenesis, residues of subunit IDH1 mutant is unable to bind AMP, ligand-binding analysis
A108R/F136Y/T241D/N245D/R114A/Y142F/D248T/D252N
-
site-directed mutagenesis, residues of subunit IDH1 are A108R, F136Y, T241D, and N245D, residues of subunit IDH2 are R114A, Y142F, D248T, and D252N, mutant is unable to bind AMP, ligand-binding analysis
C150S
C56S/C150S/C242S
-
site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme
C56S/C242S
D279A
D279A/D280A
-
site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis
D286A
D286A/I287A
-
site-directed mutagenesis, mutation of a IDH2 residue, highly reduced NAD+ binding, ligand-binding analysis
G15D
H281A
-
site-directed mutagenesis, mutation of a IDH2 residue, mutant cannot bind NAD+, ligand-binding analysis
I221A/V225A/V229A
mutant enzyme IDH1-IDH2(I221A/V225A/V229A) shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. Mutant enzyme IDH1-IDH2 (I221A/V225A/V229A) exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
I280A
I287A
R114A/Y142F/D248T/D252N
-
site-directed mutagenesis, residues of subunit subunit IDH2, ligand-binding analysis
R274A
-
site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis
S92A
S92A/S98A
-
site-directed mutagenesis, residue of subunit IDH1 is S92, residue of subunit IDH2 is S98, ligand-binding analysis
S98A
V216A/S220A/V224A
IDH1(V216A/S220A/V224A)IDH2 mutant enzyme shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. IDH1(V216A/S220A/V224A)IDH2 mutant enzyme exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
V216A/S220A/V224A/I221A/V225A/V229A
in the absence of AMP, the IDH1(V216A/S220A/V224A)-IDH2(I221A/V225A/V229A) mutant enzyme demonstrates an about 30fold decrease in apparent Vmax relative to wild-type and a loss of cooperativity with respect to isocitrate and, in the presence of AMP, the apparent affinity of the enzyme for isocitrate is 35fold lower than that of the wild-type enzyme. This mutant enzyme also exhibits a significant decrease in apparent affinity for NAD+ (about 30fold in the absence of AMP and about 10fold in the presence of AMP relative to wild-type). The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme demonstrates decreases in apparent affnity for isocitrate of about 12fold in the absence of AMP and of about 26fold in the presence of AMP relative to wild-type. For this mutant enzyme, with respect to isocitrate, allosteric activation by AMP and cooperativity in the absence of AMP are no longer apparen. The mutant enzyme is not fully functional in vivo
C150S
-
insensitive to treatment with diamide, the presence of the IDH2 Cys-150 residue (and perhaps the potential for disulfide bond formation) may contribute to cooperativity and may also limit maximal IDH activity
C150S
-
an octameric IDH1/IDH2C150S mutant enzyme, that shows unaltered activity and similar kinetics compared to the wild-type enzyme
C150S
-
site-directed mutagenesis of subunit IDH2, disulfide bridge formation by C150 is abolished
C56S/C242S
-
shows activity similar to wild type enzyme and is sensitive to treatment with diamide
C56S/C242S
-
an octameric IDH1/IDH2C56S/C242S mutant enzyme, the mutant enzyme shows a reduction in Vmax relative to that of the wild-type enzyme of about 50%, although about 30% activity is restored in the presence of dithiothreitol
C56S/C242S
-
site-directed mutagenesis of subunit IDH2, the mutation does not affect disulfide formation in the enzyme
C56S/C242S
-
site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme
D279A
-
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
D286A
-
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
G15D
-
a tetrameric IDH1G15D/IDH2 mutant enzyme, that shows reduced activity and altered kinetics compared to the wild-type enzyme
G15D
-
site-directed mutagenesis of subunit IDH1, the tetrameric IDH1G15D/IDH2 enzyme exhibits half-site binding (two sites) for isocitrate in the absence of DTT and full-site binding (four sites) in the presence of DTT
I280A
-
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
I287A
-
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
S92A
-
site-directed mutagenesis, residue of subunit IDH1, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, ligand-binding analysis
S98A
-
site-directed mutagenesis, residue of subunit IDH2, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, ligand-binding analysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, recombinant wild-type enzyme, in affinity elution buffer containing 50 mM sodium phosphate, pH 7.5, 300 mM NaCl, and 200 mM imidazole, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-nitrilotriacetate (Ni2+-NTA) column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21-Gold(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from strain IDH12DELTAL by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes are expressed in a idh1DELTAidh2DELTA yeast strain which contains deletion/insertion mutations in genomic IDH1 and IDH2 loci
expression of His-tagged wild-type and mutant enzymes in yeast strain IDH12DELTAL deficient in both subunits of the enzyme
-
His-tagged enzyme expression in Escherichia coli strain BL21-Gold(DE3)
-
wild-type and mutant enzymes are expressed in a idh1DELTAidh2DELTA yeast strain which contains deletion/insertion mutations in genomic IDH1 and IDH2 loci
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Plaut, G.W.E.
Isocitrate dehydrogenase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
105-126
1963
Aspergillus niger, Bos taurus, Saccharomyces cerevisiae, Cavia porcellus, Columba livia, Homo sapiens, Pisum sativum, Rattus norvegicus
-
Gabriel, J.L.; Plaut, G.W.E.
Kinetic regulation of yeast NAD-specific isocitrate dehydrogenase by citrate
Biochemistry
30
2594-2599
1991
Saccharomyces cerevisiae
Panisko, E.A.; McAllister-Henn, L.
Subunit interactions of yeast NAD+-specific isocitrate dehydrogenase
J. Biol. Chem.
276
1204-1210
2001
Saccharomyces cerevisiae
Anderson, S.L.; Minard, K.I.; McAllister-Henn, L.
Allosteric inhibition of NAD+-specific isocitrate dehydrogenase by a mitochondrial mRNA
Biochemistry
39
5623-5629
2000
Saccharomyces cerevisiae
Anderson, S.L.; Schirf, V.; McAlister-Henn, L.
Effect of AMP on mRNA binding by yeast NAD+-specific isocitrate dehydrogenase
Biochemistry
41
7065-7073
2002
Saccharomyces cerevisiae
Lin, A.P.; McAlister-Henn, L.
Isocitrate binding at two functionally distinct sites in yeast NAD+-specific isocitrate dehydrogenase
J. Biol. Chem.
277
22475-22483
2002
Saccharomyces cerevisiae
Lin, A.P.; McAlister-Henn, L.
Homologous binding sites in yeast isocitrate dehydrogenase for cofactor (NAD+) and allosteric activator (AMP)
J. Biol. Chem.
278
12864-12872
2003
Saccharomyces cerevisiae
Hu, G.; Taylor, A.B.; McAlister-Henn, L.; Hart, P.J.
Crystallization and preliminary x-ray crystallographic analysis of yeast NAD+-specific isocitrate dehydrogenase. [Erratum to document cited in CA143:301281]
Acta Crystallogr. Sect. F
F62
709
2006
Saccharomyces cerevisiae
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Hu, G.; McAlister-Henn, L.
Novel allosteric properties produced by residue substitutions in the subunit interface of yeast NAD+-specific isocitrate dehydrogenase
Arch. Biochem. Biophys.
453
207-216
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P28241), Saccharomyces cerevisiae (P28834), Saccharomyces cerevisiae MMY011
Anderson, S.L.; Lin, A.P.; McAlister-Henn, L.
Analysis of interactions with mitochondrial mRNA using mutant forms of yeast NAD(+)-specific isocitrate dehydrogenase
Biochemistry
44
16776-16784
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Hu, G.; Lin, A.P.; McAlister-Henn, L.
Physiological consequences of loss of allosteric activation of yeast NAD+-specific isocitrate dehydrogenase
J. Biol. Chem.
281
16935-16942
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Lin, A.P.; Hakala, K.W.; Weintraub, S.T.; McAlister-Henn, L.
Suppression of metabolic defects of yeast isocitrate dehydrogenase and aconitase mutants by loss of citrate synthase
Arch. Biochem. Biophys.
474
205-212
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Taylor, A.B.; Hu, G.; Hart, P.J.; McAlister-Henn, L.
Allosteric motions in structures of yeast NAD+-specific isocitrate dehydrogenase
J. Biol. Chem.
283
10872-10880
2008
Saccharomyces cerevisiae
Garcia, J.A.; Minard, K.I.; Lin, A.P.; McAlister-Henn, L.
Disulfide bond formation in yeast NAD+-specific isocitrate dehydrogenase
Biochemistry
48
8869-8878
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
McAlister-Henn, L.
Ligand binding and structural changes associated with allostery in yeast NAD+-specific isocitrate dehydrogenase
Arch. Biochem. Biophys.
519
112-117
2012
Saccharomyces cerevisiae
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