DB code: S00416

CATH domain 3.40.718.10 : Isopropylmalate Dehydrogenase Catalytic domain
E.C. 1.1.1.42
CSA
M-CSA
MACiE M0007

CATH domain Related DB codes (homologues)
3.40.718.10 : Isopropylmalate Dehydrogenase S00417

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q9YE81
Isocitrate dehydrogenase {NADP}
EC 1.1.1.42
NP_147421.2 (Protein)
NC_000854.2 (DNA/RNA sequence)
PF00180 (Iso_dh)
[Graphical View]
P08200 Isocitrate dehydrogenase {NADP}
IDH
EC 1.1.1.42
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
NP_415654.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489404.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00180 (Iso_dh)
[Graphical View]
P39126 Isocitrate dehydrogenase {NADP}
IDH
EC 1.1.1.42
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
NP_390791.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PF00180 (Iso_dh)
[Graphical View]
P33198 Isocitrate dehydrogenase {NADP}, mitochondrial
IDH
EC 1.1.1.42
ICD-M
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
PF00180 (Iso_dh)
[Graphical View]
O75874 Isocitrate dehydrogenase {NADP} cytoplasmic
IDH
EC 1.1.1.42
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
NP_005887.2 (Protein)
NM_005896.2 (DNA/RNA sequence)
PF00180 (Iso_dh)
[Graphical View]

KEGG enzyme name
isocitrate dehydrogenase (NADP+)
oxalosuccinate decarboxylase
oxalsuccinic decarboxylase
isocitrate (NADP) dehydrogenase
isocitrate (nicotinamide adenine dinucleotide phosphate)dehydrogenase
NADP-specific isocitrate dehydrogenase
NADP-linked isocitrate dehydrogenase
NADP-dependent isocitrate dehydrogenase
NADP isocitric dehydrogenase
isocitrate dehydrogenase (NADP-dependent)
NADP-dependent isocitric dehydrogenase
triphosphopyridine nucleotide-linked isocitratedehydrogenase-oxalosuccinate carboxylase
NADP+-linked isocitrate dehydrogenase
IDH (ambiguous)
dual-cofactor-specific isocitrate dehydrogenase
NADP+-ICDH
NADP+-IDH
IDP
IDP1
IDP2
IDP3

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9YE81 Q9YE81_AERPE
P08200 IDH_ECOLI Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Homodimer. Binds 1 magnesium or manganese ion per subunit.
P39126 IDH_BACSU Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Homodimer. Binds 1 magnesium or manganese ion per subunit (By similarity).
P33198 IDHP_PIG Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Homodimer. Mitochondrion. Binds 1 magnesium or manganese ion per subunit.
O75874 IDHC_HUMAN Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Homodimer. Cytoplasm. Peroxisome. Binds 1 magnesium or manganese ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00020 Citrate cycle (TCA cycle)
MAP00480 Glutathione metabolism
MAP00720 Reductive carboxylate cycle (CO2 fixation)

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00572 C00006 C00311 C00005 C00011 C00026 C00080 C05379
E.C.
Compound Divalent cation (Mg or Mn) NADP+ Isocitrate NADPH CO2 2-Oxoglutarate H+ Oxalosuccinate
Type divalent metal (Ca2+, Mg2+) amide group,amine group,nucleotide carbohydrate,carboxyl group amide group,amine group,nucleotide others carbohydrate,carboxyl group others
ChEBI 18009
30887
16474
16526
30915
15378
PubChem 5886
1198
5884
280
51
1038
1tyoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tyoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1v94A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1v94B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xgvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xgvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xkdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1xkdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1ai2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:ICA Bound:NAP Bound:ICA Unbound Unbound Unbound Unbound
1ai3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:ITM Analogue:NDO Bound:ITM Unbound Unbound Unbound Unbound
1bl5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Analogue:NAP Unbound Unbound Unbound Bound:AKG Unbound
1cw1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_MN Unbound Bound:ICT Unbound Unbound Unbound Unbound
1cw4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_MN Unbound Unbound Unbound Unbound Bound:AKG Unbound
1cw7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
1groA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
1grpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
1hj6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Bound:NAP Analogue:IPM Unbound Unbound Unbound Unbound
1idcA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Intermediate-bound:OXS
1iddA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ideA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1idfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ikaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Unbound Unbound Unbound Unbound Bound:AKG Unbound
1ikbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1isoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:AMP Unbound Unbound Unbound Unbound Unbound
1p8fA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
1pb1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:ICT Unbound Unbound Unbound Unbound
1pb3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sjsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
6icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
7icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
8icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:ICT Unbound Unbound Unbound Unbound
9icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:NAP Unbound Unbound Unbound Unbound Unbound
1hqsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Unbound Unbound Unbound
1hqsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Unbound Unbound Unbound
1lwdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_MN Unbound Bound:ICT Unbound Unbound Unbound Unbound
1lwdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_MN Unbound Bound:ICT Unbound Unbound Unbound Unbound
1t09A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound Unbound
1t09B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound Unbound
1t0lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1t0lB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1t0lC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound
1t0lD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CA Bound:NAP Bound:ICT Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [11], [15]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1tyoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1tyoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1v94A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1v94B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1xgvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1xgvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1xkdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1xkdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 166;LYS 233;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 120(Phosphorylation)
1ai2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1ai3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1bl5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1cw1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant K230M
1cw4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;;ASP 283 ASP 307;ASP 311(Manganese binding) SER 113(Phosphorylation) mutant K230M
1cw7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1groA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) mutant S113E, N115L
1grpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant N115L
1hj6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) mutant S113E
1idcA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant K230M
1iddA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant Y160F
1ideA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant Y160F
1idfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant K230M
1ikaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1ikbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1isoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation) mutant C201M, C332Y, K344D, Y345I, V351A, Y391K, R395S
1p8fA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1pb1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1pb3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1sjsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
3icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
4icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
5icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
6icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) mutant S113E
7icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) mutant S113E
8icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) mutant S113E
9icdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 160;LYS 230;ASP 283 ASP 307;ASP 311(Magnesium binding) SER 113(Phosphorylation)
1hqsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 151;LYS 221;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 104(Phosphorylation);CME 118
1hqsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 151;LYS 221;ASP 287 ASP 311;ASP 315(Magnesium binding) SER 104(Phosphorylation);CME 118
1lwdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 140;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 95(Phosphorylation)
1lwdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 140;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 95(Phosphorylation)
1t09A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)
1t09B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)
1t0lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)
1t0lB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)
1t0lC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)
1t0lD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 139;LYS 212;ASP 252 ASP 275;ASP 279(Magnesium binding) SER 94(Phosphorylation)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[11]
Fig.7, p.8675-8676
[13]
p.9314, p.9315-9316
[14]
Fig.1
[15]
p.382-383
[19]
Fig.25
[20]
p.292
[23]
[24]
Fig.1
[27]
[31]
Fig.7, p.43461-43462
[32]
[33]
p.33954, Fig.6
[35]
p.567-568

References
[1]
Resource
Comments
Medline ID
PubMed ID 6254771
Journal Eur J Biochem
Year 1980
Volume 110
Pages 465-73
Authors Kuchel PW, Reynolds CH, Dalziel K
Title Determination of the stability constants of Mn2+ and Mg2+ complexes of the components of the NADP-linked isocitrate dehydrogenase reaction by electron spin resonance.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6722120
Journal Biochemistry
Year 1984
Volume 23
Pages 1675-83
Authors Mas MT, Colman RF
Title Phosphorus-31 nuclear magnetic resonance studies of the binding of nucleotides to NADP+-specific isocitrate dehydrogenase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 4074702
Journal Biochemistry
Year 1985
Volume 24
Pages 5378-87
Authors Ehrlich RS, Colman RF
Title 1H nuclear magnetic resonance studies of the conformation and environment of nucleotides bound to pig heart NADP+-dependent isocitrate dehydrogenase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3651391
Journal Biochemistry
Year 1987
Volume 26
Pages 3461-6
Authors Ehrlich RS, Colman RF
Title Ionization of isocitrate bound to pig heart NADP+-dependent isocitrate dehydrogenase: 13C NMR study of substrate binding.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2753210
Journal Biochem Soc Trans
Year 1989
Volume 17
Pages 307-11
Authors Colman RF
Title Affinity labels and spectroscopic probes of porcine heart NADP-dependent isocitrate dehydrogenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2541772
Journal Biochemistry
Year 1989
Volume 28
Pages 2058-65
Authors Ehrlich RS, Colman RF
Title Multinuclear NMR studies of the divalent metal binding site of NADP-dependent isocitrate dehydrogenase from pig heart.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 90046847
PubMed ID 2682654
Journal Proc Natl Acad Sci U S A
Year 1989
Volume 86
Pages 8635-9
Authors Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM
Title Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Related PDB 3icd
Related UniProtKB P08200
[8]
Resource
Comments
Medline ID
PubMed ID 2378874
Journal Biochemistry
Year 1990
Volume 29
Pages 5179-87
Authors Ehrlich RS, Colman RF
Title Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2406256
Journal J Biol Chem
Year 1990
Volume 265
Pages 3599-602
Authors Hurley JH, Dean AM, Thorsness PE, Koshland DE Jr, Stroud RM
Title Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme.
Related PDB 4icd
Related UniProtKB
[10]
Resource
Comments INFLUENCE OF PHOSPHORYLATION
Medline ID 90371294
PubMed ID 2204109
Journal Science
Year 1990
Volume 249
Pages 1012-6
Authors Hurley JH, Dean AM, Sohl JL, Koshland DE Jr, Stroud RM
Title Regulation of an enzyme by phosphorylation at the active site.
Related PDB 5icd 6icd 7icd 8icd
Related UniProtKB P08200
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1888729
Journal Biochemistry
Year 1991
Volume 30
Pages 8671-8
Authors Hurley JH, Dean AM, Koshland DE Jr, Stroud RM
Title Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.
Related PDB 9icd
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 1463739
Journal Biochemistry
Year 1992
Volume 31
Pages 12524-31
Authors Ehrlich RS, Colman RF
Title Selectivity in the binding of NAD(P)+ analogues to NAD- and NADP-dependent pig heart isocitrate dehydrogenases. A nuclear magnetic resonance study.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8369300
Journal Biochemistry
Year 1993
Volume 32
Pages 9310-6
Authors Stoddard BL, Dean A, Koshland DE Jr
Title Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8369301
Journal Biochemistry
Year 1993
Volume 32
Pages 9317-22
Authors Stoddard BL, Koshland DE Jr
Title Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate.
Related PDB 1ika
Related UniProtKB
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7819221
Journal Biochemistry
Year 1995
Volume 34
Pages 378-84
Authors Lee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr
Title Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli.
Related PDB 1idd
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 7819280
Journal Biochim Biophys Acta
Year 1995
Volume 1246
Pages 135-41
Authors Ehrlich RS, Colman RF
Title Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7761851
Journal Science
Year 1995
Volume 268
Pages 1312-8
Authors Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL
Title Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.
Related PDB 1idc 1ide 1idf
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8639526
Journal Biochemistry
Year 1996
Volume 35
Pages 5670-8
Authors Hurley JH, Chen R, Dean AM
Title Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutant.
Related PDB 1iso
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 8888067
Journal Pharmacol Ther
Year 1996
Volume 70
Pages 215-56
Authors Stoddard BL
Title Intermediate trapping and laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8745407
Journal Protein Sci
Year 1996
Volume 5
Pages 287-95
Authors Chen R, Grobler JA, Hurley JH, Dean AM
Title Second-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase.
Related PDB 1gro 1grp
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 9220992
Journal Biochemistry
Year 1997
Volume 36
Pages 9035-44
Authors Cohen BE, Stoddard BL, Koshland DE Jr
Title Caged NADP and NAD. Synthesis and characterization of functionally distinct caged compounds.
Related PDB
Related UniProtKB
[22]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9374867
Journal Biochemistry
Year 1997
Volume 36
Pages 13890-6
Authors Finer-Moore J, Tsutakawa SE, Cherbavaz DR, LaPorte DC, Koshland DE Jr, Stroud RM
Title Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting.
Related PDB 1sjs
Related UniProtKB
[23]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9211842
Journal Science
Year 1997
Volume 277
Pages 202-6
Authors Mesecar AD, Stoddard BL, Koshland DE Jr
Title Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences.
Related PDB 1ai2 1ai3 1ikb
Related UniProtKB
[24]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9783749
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 891-7
Authors Stoddard BL, Cohen BE, Brubaker M, Mesecar AD, Koshland DE Jr
Title Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs.
Related PDB 1bl5
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 10779683
Journal Biochim Biophys Acta
Year 2000
Volume 1474
Pages 321-30
Authors Rao AV, Ramasarma T
Title NADH-dependent decavanadate reductase, an alternative activity of NADP-specific isocitrate dehydrogenase protein.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 10902579
Journal IUBMB Life
Year 2000
Volume 49
Pages 457-66
Authors Mesecar AD, Koshland DE Jr
Title Sites of binding and orientation in a four-location model for protein stereospecificity.
Related PDB 1pb3
Related UniProtKB
[27]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT MET-230
Medline ID 20090939
PubMed ID 10623532
Journal J Mol Biol
Year 2000
Volume 295
Pages 377-85
Authors Cherbavaz DB, Lee ME, Stroud RM, Koshland DE Jr
Title Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase.
Related PDB 1cw1 1cw4 1cw7
Related UniProtKB P08200
[28]
Resource
Comments
Medline ID
PubMed ID 10688187
Journal Nature
Year 2000
Volume 403
Pages 614-5
Authors Mesecar AD, Koshland DE Jr
Title A new model for protein stereospecificity.
Related PDB 1p8f 1pb1
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11284679
Journal Biochemistry
Year 2001
Volume 40
Pages 4234-41
Authors Doyle SA, Beernink PT, Koshland DE Jr
Title Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP.
Related PDB 1hj6
Related UniProtKB
[30]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
Medline ID
PubMed ID 11290745
Journal J Biol Chem
Year 2001
Volume 276
Pages 26154-63
Authors Singh SK, Matsuno K, LaPorte DC, Banaszak LJ
Title Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
Related PDB 1hqs
Related UniProtKB P39126
[31]
Resource
Comments
Medline ID
PubMed ID 12207025
Journal J Biol Chem
Year 2002
Volume 277
Pages 43454-62
Authors Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ
Title Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism.
Related PDB 1lwd
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 14512428
Journal J Biol Chem
Year 2003
Volume 278
Pages 49323-31
Authors Kim TK, Lee P, Colman RF
Title Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 15173171
Journal J Biol Chem
Year 2004
Volume 279
Pages 33946-57
Authors Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J
Title Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity.
Related PDB 1t09 1t0l
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 15146507
Journal Proteins
Year 2004
Volume 55
Pages 1087-9
Authors Jeong JJ, Sonoda T, Fushinobu S, Shoun H, Wakagi T
Title Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix.
Related PDB 1v94
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 15581899
Journal J Mol Biol
Year 2005
Volume 345
Pages 559-77
Authors Karlstrom M, Stokke R, Steen IH, Birkeland NK, Ladenstein R
Title Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability.
Related PDB 1tyo 1xgv 1xkd
Related UniProtKB

Comments
This enzyme can be inactivated by phosphorylation of Ser113 (of 5icd) (see literature [10]).
According to the literature [11], [14], this enzyme catalyzes the following reactions:
(A) Hydride transfer from substrate to NADP(+):
(B) Eliminative double-bond formation (or decarboxylation):
(C) Isomerization (shift of double-bond position):

Created Updated
2004-07-22 2009-02-26