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Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Thermus thermophilus and UniProt Accession P33197
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1.1.1.42 isocitrate dehydrogenase (NADP+)IUBMB Comments
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can 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 NAD+ but much more slowly [6,7].
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proneural
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
isocitrate dehydrogenase 1, nadp-isocitrate dehydrogenase, nadp-dependent isocitrate dehydrogenase, isocitrate dehydrogenase-1, nadp-icdh, nadp-idh, nadp+-dependent isocitrate dehydrogenase, nadp-linked isocitrate dehydrogenase, nadp-specific isocitrate dehydrogenase, nadp+-specific isocitrate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CtIDP1
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-
-
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CtIDP2
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-
-
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IDH
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-
-
-
IDP
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-
-
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isocitrate dehydrogenase (NADP)
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-
-
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isocitrate dehydrogenase (NADP-dependent)
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-
-
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isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate)
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-
-
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NADP isocitric dehydrogenase
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-
-
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NADP+-linked isocitrate dehydrogenase
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-
-
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NADP+-specific ICDH
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-
-
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NADP-dependent isocitrate dehydrogenase
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-
-
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NADP-dependent isocitric dehydrogenase
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-
-
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NADP-linked isocitrate dehydrogenase
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-
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NADP-specific isocitrate dehydrogenase
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-
-
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oxalosuccinate decarboxylase
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-
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oxalsuccinic decarboxylase
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-
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PS-NADP-IDH
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidative decarboxylation
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-
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reductive carboxylation
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
isocitrate:NADP+ oxidoreductase (decarboxylating)
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can 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 [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].
CAS REGISTRY NUMBER
COMMENTARY
9028-48-2
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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
additional information
?
-
the isocitrate molecule is located at the active site, and interacts with residues at the cleft between the large and small domain. The catalytic triad residues Lys191, Asp248 and Tyr144 are conserved and interact with isocitrate
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-
?
additional information
?
-
-
the isocitrate molecule is located at the active site, and interacts with residues at the cleft between the large and small domain. The catalytic triad residues Lys191, Asp248 and Tyr144 are conserved and interact with isocitrate
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a terminal domain involved in dimerization, a very unique domain when compared to other IDHs. The small domain and clasp domain show significant differences when compared to other IDHs of the same subfamily. The structure of TtIDH reveals the absence of helix at the clasp domain, which is mainly involved in oligomerization in other IDHs. Also, helices/beta sheets are absent in the small domain, when compared to other IDHs of the same subfamily. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers. The TtIDH structure with the terminal domain may be categorized as a first structure of a type IV subfamily
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a unique terminal domain involved in dimerization. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers
additional information
-
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a unique terminal domain involved in dimerization. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in ternary complex with citrate and cofactor NADP+, X-ray diffraction structure determination and analysis at 1.80 A resolution
sitting and hanging drop vapour diffusion method, using 100 mM cacodylate and 1.4 M sodium acetate, 10 mM citric acid , and 10 mM MnCl2, at pH 6.5-7.8 and 25°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saiki, T.; Arima, K.
Studies on NADP+-specific isocitrate dehydrogenase from an extreme thermophile, Thermus flavus AT-62
J. Biochem.
77
233-240
1975
Thermus thermophilus
Ishii, N.; Umemura, K.; Miyazaki, K.
Supramolecular complex formation and crystallization of isocitrate dehydrogenase from Thermus thermophilus HB8: preliminary studies with X-ray crystallography and atomic force microscopy
Biosci. Biotechnol. Biochem.
72
2369-2376
2008
Thermus thermophilus (P33197), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P33197)
Kumar, S.M.; Pampa, K.J.; Manjula, M.; Abdoh, M.M.; Kunishima, N.; Lokanath, N.K.
Crystal structure studies of NADP+ dependent isocitrate dehydrogenase from Thermus thermophilus exhibiting a novel terminal domain
Biochem. Biophys. Res. Commun.
449
107-113
2014
Thermus thermophilus (P33197), Thermus thermophilus
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