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1.1.1.42: isocitrate dehydrogenase (NADP+)
This is an abbreviated version, for detailed information about isocitrate dehydrogenase (NADP+), go to the full flat file.
Reaction
Synonyms
AfIDH, CgIDH, cICDH, CtIDP1, CtIDP2, cytosolic isocitrate dehydrogenase 1, cytosolic NADP(+)-dependent isocitrate dehydrogenase, cytosolic NADP+-dependent isocitrate dehydrogenase, cytosolic NADP-dependent isocitrate dehydrogenase, cytosolic NADPH-dependent isocitrate dehydrogenase, DpIDH, EcIDH, HICDH, ICD, ICD1, ICD2, icdA, ICDH, ICDH-1, IDH, IDH-I, IDH-IIa, IDH-IIb, IDH1, IDH2, IDH3, IDHP, IDP, IDP1, IDP2, IDP3, IDPA, IDPc, IDPm, isocitrate dehydrogenase, isocitrate dehydrogenase (NADP), isocitrate dehydrogenase (NADP-dependent), isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate), isocitrate dehydrogenase 1, isocitrate dehydrogenase 2, isocitrate dehydrogenase-1, isocytrate deyhdrogenase, mICDH, mitochondrial NADP+-dependent isocitrate dehydrogenase, NAD+-dependent isocitrate dehydrogenase, NADP isocitric dehydrogenase, NADP+ dependent isocitrate dehydrogenase, NADP+-dependent Ds-threo-isocitrate dehydrogenase, NADP+-dependent Ds-threo-isocitrate:NADP+ oxidoreductase, NADP+-dependent ICDH, NADP+-dependent IDH, NADP+-dependent isocitrate dehydrogenase, NADP+-ICDH, NADP+-IDH, NADP+-isocitrate dehydrogenase, NADP+-linked isocitrate dehydrogenase, NADP+-specific ICDH, NADP+-specific isocitrate dehydrogenase, NADP-dependent IDH, NADP-dependent isocitrate dehydrogenase, NADP-dependent isocitric dehydrogenase, NADP-ICDH, NADP-IDH, NADP-IDH Idp1p, NADP-isocitrate dehydrogenase, NADP-linked isocitrate dehydrogenase, NADP-specific isocitrate dehydrogenase, NADPH-dependent isocitrate dehydrogenase, oxalosuccinate decarboxylase, oxalsuccinic decarboxylase, perICDH, PS-NADP-IDH, TaIDH, TM1148, YlIDP
ECTree
1.1.1.42 isocitrate dehydrogenase (NADP+)Advanced search results
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22
13799
110
118
202
126
167
20
215
20
15
94
246
Reaction
Reaction on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+)
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
oxalosuccinate = 2-oxoglutarate + CO2
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
active site structure contains a well-ordered Mn2+-isocitrate complex, reaction mechanism
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
Tyr140 and Lys212 are required for catalytic activity, Tyr140 is the general acid that protonates the substrate after decarboxylation, Lys212 lowers as a positively charged residue the pK of the nearby ionizable group in the enzyme-substrate complex and stabilizes the carbanion formed initially on substrate decarboxylation
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
active site structure and reaction mechanism, conformational changes at the active site resulting in closed and open forms, regulatory residues are isocitrate-binding Asp279and Ser94
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
Ser95, Asn97, and Thr78 are important for the catalysis having distinguishable functions, overview
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
protonation of the enolate to form product 2-oxoglutarate is the rate-limiting step
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
overall reaction, catalytic mechanism, overview. The catalysis proceeds in three steps: (1) NADP+ reduction by the isocitrate substrate with the help of the Lys212B base, (2) beta-decarboxylation of the resulting oxalosuccinate, generating an enolate, and (3) protonation of this intermediate by Tyr139A, giving rise to the 2-oxooglutarate product. The beta-decarboxylation of oxalosuccinate is the most likely rate-limiting step. Role of Mg2+ and Asp275A, whose acid/base properties throughout the catalytic cycle lower the barrier to physiologically competent values. The catalysis takes place in a closed-conformation quaternary complex and involves significant conformational changes as the divalent metal (Mg2+ or Mn2+), the NADP+ cofactor, and the trianionic form of the isocitrate substrate (ICT) sequentially bind
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isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
protonation of the enolate to form product 2-oxoglutarate is the rate-limiting step
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Information
