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 Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP |
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 Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP |
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 Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP ICD-M |
PF00180
(Iso_dh)
[Graphical View] |
|
O75874 |
Isocitrate dehydrogenase {NADP} cytoplasmic
|
IDH
EC 1.1.1.42 Cytosolic NADP-isocitrate dehydrogenase Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP |
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 18009 |
30887 30887 |
16474 16474 |
16526 16526 |
30915 30915 |
15378 15378 |
|||||||
PubChem |
5886 5886 |
1198 1198 |
5884 5884 |
280 280 |
51 51 |
1038 1038 |
|||||||
1tyoA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1tyoB | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1v94A | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1v94B | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1xgvA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1xgvB | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1xkdA | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1xkdB | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1ai2A | Analogue:ICA | Bound:NAP | Bound:ICA | Unbound | Unbound | Unbound | Unbound | ||||||
1ai3A | Bound:ITM | Analogue:NDO | Bound:ITM | Unbound | Unbound | Unbound | Unbound | ||||||
1bl5A | Bound:_MG | Analogue:NAP | Unbound | Unbound | Unbound | Bound:AKG | Unbound | ||||||
1cw1A | Analogue:_MN | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1cw4A | Analogue:_MN | Unbound | Unbound | Unbound | Unbound | Bound:AKG | Unbound | ||||||
1cw7A | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1groA | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1grpA | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1hj6A | Bound:_MG | Bound:NAP | Analogue:IPM | Unbound | Unbound | Unbound | Unbound | ||||||
1idcA | Bound:_MG | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:OXS | ||||||
1iddA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ideA | Bound:_MG | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1idfA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ikaA | Analogue:_CA | Unbound | Unbound | Unbound | Unbound | Bound:AKG | Unbound | ||||||
1ikbA | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1isoA | Unbound | Analogue:AMP | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1p8fA | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1pb1A | Unbound | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1pb3A | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1sjsA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3icdA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4icdA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5icdA | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
6icdA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
7icdA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
8icdA | Bound:_MG | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
9icdA | Unbound | Analogue:NAP | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1hqsA | Unbound | Unbound | Analogue:CIT | Unbound | Unbound | Unbound | Unbound | ||||||
1hqsB | Unbound | Unbound | Analogue:CIT | Unbound | Unbound | Unbound | Unbound | ||||||
1lwdA | Analogue:_MN | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1lwdB | Analogue:_MN | Unbound | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1t09A | Unbound | Bound:NAP | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1t09B | Unbound | Bound:NAP | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1t0lA | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1t0lB | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1t0lC | Analogue:_CA | Bound:NAP | Bound:ICT | Unbound | Unbound | Unbound | Unbound | ||||||
1t0lD | 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 | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1tyoB | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1v94A | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1v94B | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1xgvA | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1xgvB | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1xkdA | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1xkdB | TYR 166;LYS 233;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 120(Phosphorylation) | |||||||
1ai2A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1ai3A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1bl5A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1cw1A | TYR 160;;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant K230M | ||||||
1cw4A | TYR 160;;ASP 283 | ASP 307;ASP 311(Manganese binding) | SER 113(Phosphorylation) | mutant K230M | ||||||
1cw7A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1groA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | mutant S113E, N115L | |||||||
1grpA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant N115L | ||||||
1hj6A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | mutant S113E | |||||||
1idcA | TYR 160;;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant K230M | ||||||
1iddA | ;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant Y160F | ||||||
1ideA | ;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant Y160F | ||||||
1idfA | TYR 160;;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant K230M | ||||||
1ikaA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1ikbA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1isoA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | mutant C201M, C332Y, K344D, Y345I, V351A, Y391K, R395S | ||||||
1p8fA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1pb1A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1pb3A | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1sjsA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
3icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
4icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
5icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
6icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | mutant S113E | |||||||
7icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | mutant S113E | |||||||
8icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | mutant S113E | |||||||
9icdA | TYR 160;LYS 230;ASP 283 | ASP 307;ASP 311(Magnesium binding) | SER 113(Phosphorylation) | |||||||
1hqsA | TYR 151;LYS 221;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 104(Phosphorylation);CME 118 | |||||||
1hqsB | TYR 151;LYS 221;ASP 287 | ASP 311;ASP 315(Magnesium binding) | SER 104(Phosphorylation);CME 118 | |||||||
1lwdA | TYR 140;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 95(Phosphorylation) | |||||||
1lwdB | TYR 140;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 95(Phosphorylation) | |||||||
1t09A | TYR 139;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 94(Phosphorylation) | |||||||
1t09B | TYR 139;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 94(Phosphorylation) | |||||||
1t0lA | TYR 139;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 94(Phosphorylation) | |||||||
1t0lB | TYR 139;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 94(Phosphorylation) | |||||||
1t0lC | TYR 139;LYS 212;ASP 252 | ASP 275;ASP 279(Magnesium binding) | SER 94(Phosphorylation) | |||||||
1t0lD | 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, |
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, |
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. |
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, |
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, |
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. |
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, |
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, |
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. |
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. |
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], (A) Hydride transfer from substrate to NADP(+): (B) Eliminative double-bond formation (or decarboxylation): (C) Isomerization (shift of double-bond position): |
Created | Updated |
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2004-07-22 | 2009-02-26 |