Crystallographic structure of E. coli isocitrate dehydrogenase.[1] There are three active sites. Three isocitrates, one isocitrate in the binding site for NADP+.
Identifiers
EC no.
1.1.1.42
CAS no.
9028-48-2
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
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articles
PubMed
articles
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proteins
isocitrate dehydrogenase (NAD+)
Identifiers
EC no.
1.1.1.41
CAS no.
9001-58-5
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
PMC
articles
PubMed
articles
NCBI
proteins
Monomeric isocitrate dehydrogenase
crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and mn
Identifiers
Symbol
IDH
Pfam
PF03971
Pfam clan
CL0270
InterPro
IPR004436
SCOP2
1ofg / SCOPe / SUPFAM
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms: IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.[2]
^PDB: 1CW7; Cherbavaz DB, Lee ME, Stroud RM, Koshland DE (January 2000). "Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase". Journal of Molecular Biology. 295 (3): 377–385. doi:10.1006/jmbi.1999.3195. PMID 10623532.
Isocitratedehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate...
Isocitratedehydrogenase [NADP], mitochondrial is an enzyme that in humans is encoded by the IDH2 gene. Isocitratedehydrogenases are enzymes that catalyze...
Isocitratedehydrogenase 1 (NADP+), soluble is an enzyme that in humans is encoded by the IDH1 gene on chromosome 2. Isocitratedehydrogenases catalyze...
all dehydrogenases in the citric acid cycle with the exception of succinate dehydrogenase, inhibits pyruvate dehydrogenase, isocitratedehydrogenase, α-ketoglutarate...
Isocitratedehydrogenase [NAD] subunit alpha, mitochondrial (IDH3α) is an enzyme that in humans is encoded by the IDH3A gene. Isocitrate dehydrogenases...
glioma. It is a small molecule inhibitor of isocitratedehydrogenase-1 (IDH1) and isocitratedehydrogenase-2 (IDH2), which are mutated in several forms...
understand the characteristics of the isocitratedehydrogenase ancestral protein. The mutant isocitratedehydrogenase genes contain inferred ancestral sequences...
phosphorylation of isocitratedehydrogenase, which has a much higher affinity for isocitrate as compared to ICL. Deactivation of isocitratedehydrogenase by phosphorylation...
acid is a substrate of the citric acid cycle. It is acted upon by isocitratedehydrogenase. Salts and esters of oxalosuccinic acid are known as oxalosuccinates...
Isocitratedehydrogenase [NAD] subunit beta, mitochondrial is an enzyme that in humans is encoded by the IDH3B gene. Isocitratedehydrogenases (IDHs) catalyze...
processes are NADP-linked isoforms of malic enzyme, isocitratedehydrogenase (IDH), and glutamate dehydrogenase. In these reactions, NADP+ acts like NAD+ in...
synthase, isocitratedehydrogenase, α-ketoglutarate dehydrogenase, fumarase, and malate dehydrogenase) except for succinate dehydrogenase which is on...
Isocitratedehydrogenase [NAD] subunit gamma, mitochondrial is an enzyme that in humans is encoded by the IDH3G gene. Isocitratedehydrogenases (IDHs)...
citrate with the help of the enzyme aconitase, and is acted upon by isocitratedehydrogenase. Isocitric acid is commonly used as a marker to detect the authenticity...
frequencies of mutation. Mutations in gliomas frequently occur in either isocitratedehydrogenase (IDH) 1 or 2 genes. One of these mutations (mostly in IDH1) occurs...
sorbitol dehydrogenase TCA cycle examples: isocitratedehydrogenase (uses NAD+, also has an isozyme that uses NADP) alpha-ketoglutarate dehydrogenase (uses...
the DNA damage response. The IDH1 gene encodes for the enzyme isocitratedehydrogenase 1 and is not mutated in glioblastoma. As such, these tumors behave...
leukemia with a susceptible IDH1 mutation. Olutasidenib is an isocitratedehydrogenase-1 (IDH1) inhibitor. It is taken by mouth. The most common adverse...
the TCA cycle of cancer cells by inhibiting isocitratedehydrogenase-1 (IDH1) and isocitratedehydrogenase-2 (IDH2), respectively. Ivosidenib is specific...
inhibitor of isocitratedehydrogenase-1 (IDH1), which is mutated in several forms of cancer. Ivosidenib is an isocitratedehydrogenase-1 inhibitor that...
acute myeloid leukemia in people with specific mutations of the isocitratedehydrogenase 2 (IDH2) gene, determined by an FDA-approved IDH2 companion diagnostic...
have more ring sideroblasts. Mutations in the genes encoding for isocitratedehydrogenase 1 and 2 (IDH1 and IDH2) occur in 10–20% of patients with myelodysplastic...
FDA-approved test. Ivodesinib (Tibsovo) is a small molecule inhibitor of isocitratedehydrogenase 1. The FDA approved ivosidenib in August 2021 for adults with previously...
Feng Y, Xiong Y, Qiao T, Li X, Jia L, Han Y (December 2018). "Lactate dehydrogenase A: A key player in carcinogenesis and potential target in cancer therapy"...
Other types of mutations in proteins such as isocitratedehydrogenase 1 (IDH1) and isocitratedehydrogenase 2 (IDH2) can cause the inactivation of histone...
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