EzCatDB: S00416
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DB codeS00416
CATH domainDomain 13.40.718.10 : Isopropylmalate DehydrogenaseCatalytic domain
E.C.1.1.1.42
MACiEM0007

CATH domainRelated DB codes (homologues)
3.40.718.10 : Isopropylmalate DehydrogenaseS00417

Enzyme Name
UniProtKBKEGG

Q9YE81P08200P39126P33198O75874
Protein name
Isocitrate dehydrogenase {NADP}Isocitrate dehydrogenase {NADP}Isocitrate dehydrogenase {NADP}, mitochondrialIsocitrate dehydrogenase {NADP} cytoplasmicisocitrate 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
SynonymsIsocitrate dehydrogenase {NADP}
EC 1.1.1.42
IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
ICD-M
IDH
EC 1.1.1.42
Cytosolic NADP-isocitrate dehydrogenase
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
RefSeqNP_147421.2 (Protein)
NC_000854.2 (DNA/RNA sequence)
NP_415654.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489404.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
NP_390791.1 (Protein)
NC_000964.3 (DNA/RNA sequence)

NP_005887.2 (Protein)
NM_005896.2 (DNA/RNA sequence)
PfamPF00180 (Iso_dh)
[Graphical view]
PF00180 (Iso_dh)
[Graphical view]
PF00180 (Iso_dh)
[Graphical view]
PF00180 (Iso_dh)
[Graphical view]
PF00180 (Iso_dh)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00020Citrate cycle (TCA cycle)
MAP00480Glutathione metabolism
MAP00720Reductive carboxylate cycle (CO2 fixation)

UniProtKB:Accession NumberQ9YE81P08200P39126P33198O75874
Entry nameQ9YE81_AERPEIDH_ECOLIIDH_BACSUIDHP_PIGIDHC_HUMAN
Activity
Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.,Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.,Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.,Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.,Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.
Subunit
Homodimer.Homodimer.Homodimer.Homodimer.
Subcellular location


Mitochondrion.Cytoplasm. Peroxisome.
Cofactor
Binds 1 magnesium or manganese ion per subunit.Binds 1 magnesium or manganese ion per subunit (By similarity).Binds 1 magnesium or manganese ion per subunit.Binds 1 magnesium or manganese ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00572C00006C00311C00005C00011C00026C00080C05379
CompoundDivalent cation (Mg or Mn)NADP+IsocitrateNADPHCO22-OxoglutarateH+Oxalosuccinate
Typedivalent metal (Ca2+, Mg2+)amide group,amine group,nucleotidecarbohydrate,carboxyl groupamide group,amine group,nucleotideotherscarbohydrate,carboxyl groupothers
ChEBI
18009
30887
16474
16526
30915
15378

PubChem
5886
1198
5884
280
51
1038

                
1tyoAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1tyoBUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1v94AUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1v94BUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1xgvAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1xgvBUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1xkdAAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1xkdBAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1ai2AAnalogue:ICABound:NAPBound:ICAUnboundUnboundUnbound Unbound
1ai3ABound:ITMAnalogue:NDOBound:ITMUnboundUnboundUnbound Unbound
1bl5ABound:_MGAnalogue:NAPUnboundUnboundUnboundBound:AKG Unbound
1cw1AAnalogue:_MNUnboundBound:ICTUnboundUnboundUnbound Unbound
1cw4AAnalogue:_MNUnboundUnboundUnboundUnboundBound:AKG Unbound
1cw7ABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
1groABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
1grpABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
1hj6ABound:_MGBound:NAPAnalogue:IPMUnboundUnboundUnbound Unbound
1idcABound:_MGUnboundUnboundUnboundUnboundUnbound Intermediate-bound:OXS
1iddAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1ideABound:_MGBound:NAPBound:ICTUnboundUnboundUnbound Unbound
1idfAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1ikaAAnalogue:_CAUnboundUnboundUnboundUnboundBound:AKG Unbound
1ikbAAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1isoAUnboundAnalogue:AMPUnboundUnboundUnboundUnbound Unbound
1p8fABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
1pb1AUnboundUnboundBound:ICTUnboundUnboundUnbound Unbound
1pb3AUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1sjsAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
3icdAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
4icdAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
5icdABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
6icdAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
7icdAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
8icdABound:_MGUnboundBound:ICTUnboundUnboundUnbound Unbound
9icdAUnboundAnalogue:NAPUnboundUnboundUnboundUnbound Unbound
1hqsAUnboundUnboundAnalogue:CITUnboundUnboundUnbound Unbound
1hqsBUnboundUnboundAnalogue:CITUnboundUnboundUnbound Unbound
1lwdAAnalogue:_MNUnboundBound:ICTUnboundUnboundUnbound Unbound
1lwdBAnalogue:_MNUnboundBound:ICTUnboundUnboundUnbound Unbound
1t09AUnboundBound:NAPUnboundUnboundUnboundUnbound Unbound
1t09BUnboundBound:NAPUnboundUnboundUnboundUnbound Unbound
1t0lAAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1t0lBAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1t0lCAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound
1t0lDAnalogue:_CABound:NAPBound:ICTUnboundUnboundUnbound Unbound

Active-site residues
resource
literature [11], [15]
pdbCatalytic residuesCofactor-binding residuesModified residuescomment
            
1tyoATYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1tyoBTYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1v94ATYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1v94BTYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1xgvATYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1xgvBTYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1xkdATYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1xkdBTYR 166;LYS 233;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 120(Phosphorylation)
 
1ai2ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1ai3ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1bl5ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1cw1ATYR 160;       ;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
mutant K230M
1cw4ATYR 160;       ;ASP 283
ASP 307;ASP 311(Manganese binding)
SER 113(Phosphorylation)
mutant K230M
1cw7ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1groATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
                        
mutant S113E, N115L
1grpATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
mutant N115L
1hj6ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
                        
mutant S113E
1idcATYR 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
1idfATYR 160;       ;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
mutant K230M
1ikaATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1ikbATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1isoATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
mutant C201M, C332Y, K344D, Y345I, V351A, Y391K, R395S
1p8fATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1pb1ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1pb3ATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1sjsATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
3icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
4icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
5icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
6icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
                        
mutant S113E
7icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
                        
mutant S113E
8icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
                        
mutant S113E
9icdATYR 160;LYS 230;ASP 283
ASP 307;ASP 311(Magnesium binding)
SER 113(Phosphorylation)
 
1hqsATYR 151;LYS 221;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 104(Phosphorylation);CME 118
 
1hqsBTYR 151;LYS 221;ASP 287
ASP 311;ASP 315(Magnesium binding)
SER 104(Phosphorylation);CME 118
 
1lwdATYR 140;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  95(Phosphorylation)
 
1lwdBTYR 140;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  95(Phosphorylation)
 
1t09ATYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 
1t09BTYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 
1t0lATYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 
1t0lBTYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 
1t0lCTYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 
1t0lDTYR 139;LYS 212;ASP 252
ASP 275;ASP 279(Magnesium binding)
SER  94(Phosphorylation)
 

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID6254771
JournalEur J Biochem
Year1980
Volume110
Pages465-73
AuthorsKuchel PW, Reynolds CH, Dalziel K
TitleDetermination of the stability constants of Mn2+ and Mg2+ complexes of the components of the NADP-linked isocitrate dehydrogenase reaction by electron spin resonance.
[2]
PubMed ID6722120
JournalBiochemistry
Year1984
Volume23
Pages1675-83
AuthorsMas MT, Colman RF
TitlePhosphorus-31 nuclear magnetic resonance studies of the binding of nucleotides to NADP+-specific isocitrate dehydrogenase.
[3]
PubMed ID4074702
JournalBiochemistry
Year1985
Volume24
Pages5378-87
AuthorsEhrlich RS, Colman RF
Title1H nuclear magnetic resonance studies of the conformation and environment of nucleotides bound to pig heart NADP+-dependent isocitrate dehydrogenase.
[4]
PubMed ID3651391
JournalBiochemistry
Year1987
Volume26
Pages3461-6
AuthorsEhrlich RS, Colman RF
TitleIonization of isocitrate bound to pig heart NADP+-dependent isocitrate dehydrogenase: 13C NMR study of substrate binding.
[5]
PubMed ID2753210
JournalBiochem Soc Trans
Year1989
Volume17
Pages307-11
AuthorsColman RF
TitleAffinity labels and spectroscopic probes of porcine heart NADP-dependent isocitrate dehydrogenase.
[6]
PubMed ID2541772
JournalBiochemistry
Year1989
Volume28
Pages2058-65
AuthorsEhrlich RS, Colman RF
TitleMultinuclear NMR studies of the divalent metal binding site of NADP-dependent isocitrate dehydrogenase from pig heart.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID90046847
PubMed ID2682654
JournalProc Natl Acad Sci U S A
Year1989
Volume86
Pages8635-9
AuthorsHurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM
TitleStructure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Related PDB3icd
Related UniProtKBP08200
[8]
PubMed ID2378874
JournalBiochemistry
Year1990
Volume29
Pages5179-87
AuthorsEhrlich RS, Colman RF
TitleConformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart.
[9]
CommentsX-ray crystallography
PubMed ID2406256
JournalJ Biol Chem
Year1990
Volume265
Pages3599-602
AuthorsHurley JH, Dean AM, Thorsness PE, Koshland DE Jr, Stroud RM
TitleRegulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme.
Related PDB4icd
[10]
CommentsINFLUENCE OF PHOSPHORYLATION
Medline ID90371294
PubMed ID2204109
JournalScience
Year1990
Volume249
Pages1012-6
AuthorsHurley JH, Dean AM, Sohl JL, Koshland DE Jr, Stroud RM
TitleRegulation of an enzyme by phosphorylation at the active site.
Related PDB5icd,6icd,7icd,8icd
Related UniProtKBP08200
[11]
CommentsX-ray crystallography
PubMed ID1888729
JournalBiochemistry
Year1991
Volume30
Pages8671-8
AuthorsHurley JH, Dean AM, Koshland DE Jr, Stroud RM
TitleCatalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.
Related PDB9icd
[12]
PubMed ID1463739
JournalBiochemistry
Year1992
Volume31
Pages12524-31
AuthorsEhrlich RS, Colman RF
TitleSelectivity in the binding of NAD(P)+ analogues to NAD- and NADP-dependent pig heart isocitrate dehydrogenases. A nuclear magnetic resonance study.
[13]
PubMed ID8369300
JournalBiochemistry
Year1993
Volume32
Pages9310-6
AuthorsStoddard BL, Dean A, Koshland DE Jr
TitleStructure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex.
[14]
CommentsX-ray crystallography
PubMed ID8369301
JournalBiochemistry
Year1993
Volume32
Pages9317-22
AuthorsStoddard BL, Koshland DE Jr
TitleStructure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate.
Related PDB1ika
[15]
CommentsX-ray crystallography
PubMed ID7819221
JournalBiochemistry
Year1995
Volume34
Pages378-84
AuthorsLee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr
TitleMutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli.
Related PDB1idd
[16]
PubMed ID7819280
JournalBiochim Biophys Acta
Year1995
Volume1246
Pages135-41
AuthorsEhrlich RS, Colman RF
TitleCadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart.
[17]
CommentsX-ray crystallography
PubMed ID7761851
JournalScience
Year1995
Volume268
Pages1312-8
AuthorsBolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL
TitleMutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.
Related PDB1idc,1ide,1idf
[18]
CommentsX-ray crystallography
PubMed ID8639526
JournalBiochemistry
Year1996
Volume35
Pages5670-8
AuthorsHurley JH, Chen R, Dean AM
TitleDeterminants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutant.
Related PDB1iso
[19]
PubMed ID8888067
JournalPharmacol Ther
Year1996
Volume70
Pages215-56
AuthorsStoddard BL
TitleIntermediate trapping and laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening.
[20]
CommentsX-ray crystallography
PubMed ID8745407
JournalProtein Sci
Year1996
Volume5
Pages287-95
AuthorsChen R, Grobler JA, Hurley JH, Dean AM
TitleSecond-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase.
Related PDB1gro,1grp
[21]
PubMed ID9220992
JournalBiochemistry
Year1997
Volume36
Pages9035-44
AuthorsCohen BE, Stoddard BL, Koshland DE Jr
TitleCaged NADP and NAD. Synthesis and characterization of functionally distinct caged compounds.
[22]
CommentsX-ray crystallography
PubMed ID9374867
JournalBiochemistry
Year1997
Volume36
Pages13890-6
AuthorsFiner-Moore J, Tsutakawa SE, Cherbavaz DR, LaPorte DC, Koshland DE Jr, Stroud RM
TitleAccess to phosphorylation in isocitrate dehydrogenase may occur by domain shifting.
Related PDB1sjs
[23]
CommentsX-ray crystallography
PubMed ID9211842
JournalScience
Year1997
Volume277
Pages202-6
AuthorsMesecar AD, Stoddard BL, Koshland DE Jr
TitleOrbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences.
Related PDB1ai2,1ai3,1ikb
[24]
CommentsX-ray crystallography
PubMed ID9783749
JournalNat Struct Biol
Year1998
Volume5
Pages891-7
AuthorsStoddard BL, Cohen BE, Brubaker M, Mesecar AD, Koshland DE Jr
TitleMillisecond Laue structures of an enzyme-product complex using photocaged substrate analogs.
Related PDB1bl5
[25]
PubMed ID10779683
JournalBiochim Biophys Acta
Year2000
Volume1474
Pages321-30
AuthorsRao AV, Ramasarma T
TitleNADH-dependent decavanadate reductase, an alternative activity of NADP-specific isocitrate dehydrogenase protein.
[26]
PubMed ID10902579
JournalIUBMB Life
Year2000
Volume49
Pages457-66
AuthorsMesecar AD, Koshland DE Jr
TitleSites of binding and orientation in a four-location model for protein stereospecificity.
Related PDB1pb3
[27]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT MET-230
Medline ID20090939
PubMed ID10623532
JournalJ Mol Biol
Year2000
Volume295
Pages377-85
AuthorsCherbavaz DB, Lee ME, Stroud RM, Koshland DE Jr
TitleActive site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase.
Related PDB1cw1,1cw4,1cw7
Related UniProtKBP08200
[28]
PubMed ID10688187
JournalNature
Year2000
Volume403
Pages614-5
AuthorsMesecar AD, Koshland DE Jr
TitleA new model for protein stereospecificity.
Related PDB1p8f,1pb1
[29]
CommentsX-ray crystallography
PubMed ID11284679
JournalBiochemistry
Year2001
Volume40
Pages4234-41
AuthorsDoyle SA, Beernink PT, Koshland DE Jr
TitleStructural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP.
Related PDB1hj6
[30]
CommentsX-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
PubMed ID11290745
JournalJ Biol Chem
Year2001
Volume276
Pages26154-63
AuthorsSingh SK, Matsuno K, LaPorte DC, Banaszak LJ
TitleCrystal 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 PDB1hqs
Related UniProtKBP39126
[31]
PubMed ID12207025
JournalJ Biol Chem
Year2002
Volume277
Pages43454-62
AuthorsCeccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ
TitleCrystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism.
Related PDB1lwd
[32]
PubMed ID14512428
JournalJ Biol Chem
Year2003
Volume278
Pages49323-31
AuthorsKim TK, Lee P, Colman RF
TitleCritical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase.
[33]
PubMed ID15173171
JournalJ Biol Chem
Year2004
Volume279
Pages33946-57
AuthorsXu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J
TitleStructures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity.
Related PDB1t09,1t0l
[34]
PubMed ID15146507
JournalProteins
Year2004
Volume55
Pages1087-9
AuthorsJeong JJ, Sonoda T, Fushinobu S, Shoun H, Wakagi T
TitleCrystal structure of isocitrate dehydrogenase from Aeropyrum pernix.
Related PDB1v94
[35]
PubMed ID15581899
JournalJ Mol Biol
Year2005
Volume345
Pages559-77
AuthorsKarlstrom M, Stokke R, Steen IH, Birkeland NK, Ladenstein R
TitleIsocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability.
Related PDB1tyo,1xgv,1xkd

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):

createdupdated
2004-07-222009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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