EzCatDB: S00215
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00215
CATH domainDomain 13.20.20.70 : TIM BarrelCatalytic domain
E.C.1.1.1.205

CATH domainRelated DB codes (homologues)
3.20.20.70 : TIM BarrelS00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
UniProtKBKEGG

P49058Q9X168P0C0H6P50097P12269P20839P12268
Protein nameInosine-5''-monophosphate dehydrogenase
Inosine-5''-monophosphate dehydrogenaseInosine-5''-monophosphate dehydrogenaseInosine-5''-monophosphate dehydrogenase 2Inosine-5''-monophosphate dehydrogenase 1Inosine-5''-monophosphate dehydrogenase 2IMP dehydrogenase
inosine-5'-phosphate dehydrogenase
inosinic acid dehydrogenase
inosinate dehydrogenase
inosine 5'-monophosphate dehydrogenase
inosine monophosphate dehydrogenase
IMP oxidoreductase
inosine monophosphate oxidoreductase
SynonymsIMP dehydrogenase
IMPDH
IMPD
EC 1.1.1.205
Inosine-5''-monophosphate dehydrogenase
IMP dehydrogenase
IMPDH
IMPD
EC 1.1.1.205
IMP dehydrogenase
IMPDH
IMPD
EC 1.1.1.205
IMP dehydrogenase 2
EC 1.1.1.205
IMPDH-II
IMPD 2
IMP dehydrogenase 1
EC 1.1.1.205
IMPDH-I
IMPD 1
IMP dehydrogenase 2
EC 1.1.1.205
IMPDH-II
IMPD 2
RefSeqNP_047003.1 (Protein)
NC_001903.1 (DNA/RNA sequence)
NP_229148.1 (Protein)
NC_000853.1 (DNA/RNA sequence)


NP_001233751.1 (Protein)
NM_001246822.1 (DNA/RNA sequence)
NP_000874.2 (Protein)
NM_000883.3 (DNA/RNA sequence)
NP_001096075.1 (Protein)
NM_001102605.1 (DNA/RNA sequence)
NP_001136045.1 (Protein)
NM_001142573.1 (DNA/RNA sequence)
NP_001136046.1 (Protein)
NM_001142574.1 (DNA/RNA sequence)
NP_001136047.1 (Protein)
NM_001142575.1 (DNA/RNA sequence)
NP_001136048.1 (Protein)
NM_001142576.1 (DNA/RNA sequence)
NP_899066.1 (Protein)
NM_183243.2 (DNA/RNA sequence)
NP_000875.2 (Protein)
NM_000884.2 (DNA/RNA sequence)
PfamPF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism
MAP00983Drug metabolism - other enzymes

UniProtKB:Accession NumberP49058Q9X168P0C0H6P50097P12269P20839P12268
Entry nameIMDH_BORBUQ9X168_THEMAIMDH_STRPYIMDH_TRIFOIMDH2_CRIGRIMDH1_HUMANIMDH2_HUMAN
ActivityInosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH.Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.
Subunit

Homotetramer.Homotetramer.Homotetramer.Homotetramer.Homotetramer.
Subcellular location






Cofactor



Potassium.Potassium (By similarity).Potassium.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00238C00130C00003C00001C00655C00004
CompoundPotassiumInosine 5'-phosphateNAD+H2OXanthosine 5'-phosphateNADHEnzyme-Cys-IMP
Typeunivalent metal (Na+, K+)amide group,nucleotideamide group,amine group,nucleotideH2Oamide group,nucleotideamide group,amine group,nucleotide
ChEBI29103
17202
15846
15377
15652
16908

PubChem813
8582
5893
962
22247451
73323
439153

               
1eepAUnboundUnboundUnbound UnboundUnboundUnbound
1eepBUnboundUnboundUnbound UnboundUnboundUnbound
1vrdAUnboundUnboundUnbound UnboundUnboundUnbound
1vrdBUnboundUnboundUnbound UnboundUnboundUnbound
1zfjAUnboundBound:IMPUnbound UnboundUnboundUnbound
1ak5AUnboundUnboundUnbound UnboundUnboundUnbound
1lrtAUnboundBound:IMPAnalogue:TAD UnboundUnboundUnbound
1lrtBUnboundBound:IMPAnalogue:TAD UnboundUnboundUnbound
1lrtCUnboundBound:IMPAnalogue:TAD UnboundUnboundUnbound
1lrtDUnboundBound:IMPAnalogue:TAD UnboundUnboundUnbound
1me7AAnalogue:_NAAnalogue:RVPAnalogue:MOA UnboundUnboundUnbound
1me8AAnalogue:_NAAnalogue:RVPUnbound UnboundUnboundUnbound
1me9AUnboundBound:IMPUnbound UnboundUnboundUnbound
1mehAUnboundBound:IMPAnalogue:MOA UnboundUnboundUnbound
1meiAUnboundUnboundAnalogue:MOA Bound:XMPUnboundUnbound
1mewAUnboundUnboundBound:NAD Bound:XMPUnboundUnbound
1mwfABound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1mwfBBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1mwfCBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1mwfDBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1pvnABound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1pvnBBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1pvnCBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1pvnDBound:__KAnalogue:MZPUnbound UnboundUnboundUnbound
1jr1ABound:__KUnboundAnalogue:MOA UnboundUnboundIntermediate-bound:CYS 331-IMP
1jr1BBound:__KBound:IMPAnalogue:MOA UnboundUnboundUnbound
1jcnAUnboundUnboundUnbound UnboundUnboundIntermediate-analogue:CYS 331-CPR
1jcnBUnboundUnboundUnbound UnboundUnboundIntermediate-analogue:CYS 331-CPR
1b3oAUnboundAnalogue:CPRAnalogue:SAE UnboundUnboundUnbound
1b3oBUnboundUnboundAnalogue:SAE UnboundUnboundIntermediate-analogue:CYS 331-CPR
1nfbAUnboundUnboundBound:NAD UnboundUnboundIntermediate-analogue:CYS 331-CPR
1nfbBUnboundUnboundBound:NAD UnboundUnboundIntermediate-analogue:CYS 331-CPR
1nf7ABound:__KAnalogue:RVPAnalogue:MYD UnboundUnboundUnbound
1nf7BBound:__KAnalogue:RVPAnalogue:MYD UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P12268, P49058, P0C0H6, P50097 & PDB;1zfj
pdbCatalytic residuesCofactor-binding residuesModified residuescomment
            
1eepAASP 172;ASN 201;LYS 220;CYS 229;THR 231
GLY 224;GLY 226(Potassium binding)
 
 
1eepBASP 172;ASN 201;LYS 220;CYS 229;THR 231
GLY 224;GLY 226(Potassium binding)
 
 
1vrdAASP 244;ASN 273;LYS 292;CYS 301;THR 303
GLY 296;GLY 298(Potassium binding)
 
 
1vrdBASP 244;ASN 273;LYS 292;CYS 301;THR 303
GLY 296;GLY 298(Potassium binding)
 
 
1zfjAASP 253;ASN 282;LYS 301;CYS 310;THR 312
GLY 305;GLY 307(Potassium binding)
MSE 53;MSE 61;MSE 78;MSE 117;MSE 145;MSE 159;MSE 364;MSE 368;MSE 393;MSE 399;MSE 440;MSE 448;MSE 468(modified by Selenium)
 
1ak5AASP 261;ASN 291;LYS 310;       ;       
       ;                          
 
invisible 314-327
1lrtAASP 261;ASN 291;LYS 310;CYS 319;       
GLY 314;GLY 316(Potassium binding)
 
invisible 320-322
1lrtBASP 261;ASN 291;LYS 310;CYS 319;       
GLY 314;GLY 316(Potassium binding)
 
invisible 320-322
1lrtCASP 261;ASN 291;LYS 310;CYS 319;       
GLY 314;GLY 316(Potassium binding)
 
invisible 320-322
1lrtDASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1me7AASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1me8AASP 261;ASN 291;LYS 310;       ;THR 321
GLY 314;GLY 316(Potassium binding)
CSO 319(S-hydroxylated)
 
1me9AASP 261;ASN 291;LYS 310;       ;THR 321
GLY 314;GLY 316(Potassium binding)
CSO 319(S-hydroxylated)
 
1mehAASP 261;ASN 291;LYS 310;       ;THR 321
GLY 314;GLY 316(Potassium binding)
CSO 319(S-hydroxylated)
 
1meiAASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1mewAASP 261;ASN 291;       ;       
GLY 314;GLY 316(Potassium binding)
 
invisible 318-321
1mwfAASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1mwfBASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1mwfCASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1mwfDASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1pvnAASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1pvnBASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1pvnCASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1pvnDASP 261;ASN 291;LYS 310;CYS 319;THR 321
GLY 314;GLY 316(Potassium binding)
 
 
1jr1AASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1jr1BASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1jcnAASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1jcnBASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1b3oAASP 274;ASN 303;ARG 322;       ;       
GLY 326;       (Potassium binding)
 
invisible 110-231/328-340/401-448
1b3oBASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
invisible 160-177/401-448
1nfbAASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1nfbBASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1nf7AASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 
1nf7BASP 274;ASN 303;ARG 322;CYS 331;THR 333
GLY 326;GLY 328(Potassium binding)
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Scheme 1, Scheme 2
[9]p.927
[11]SCHEME II
[12]

[13]

[16]Fig.1, p.4438
[17]p.4697, p.4699-4700
[19]Scheme 1, p.617
[22]Fig.1
[23]Fig.2
[25]Fig.1, p.13315-13316
[26]Fig.1, p.36-37
[29]p.50657-50659
[30]Fig. 1, p.861-862

references
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Year1990
Volume33
Pages572-6
AuthorsRiley TA, Larson SB, Avery TL, Finch RA, Robins RK
Title1,2,4-Diazaphosphole nucleosides. Synthesis, structure, and antitumor activity of nucleosides with a lambda 3 phosphorus atom.
[2]
PubMed ID1357174
JournalJ Med Chem
Year1992
Volume35
Pages3560-7
AuthorsLi H, Goldstein BM
TitleCarboxamide group conformation in the nicotinamide and thiazole-4-carboxamide rings: implications for enzyme binding.
[3]
PubMed ID7903306
JournalJ Biol Chem
Year1993
Volume268
Pages27286-90
AuthorsCarr SF, Papp E, Wu JC, Natsumeda Y
TitleCharacterization of human type I and type II IMP dehydrogenases.
[4]
PubMed ID7906542
JournalBiochemistry
Year1994
Volume33
Pages1753-9
AuthorsAntonino LC, Wu JC
TitleHuman IMP dehydrogenase catalyzes the dehalogenation of 2-fluoro- and 2-chloroinosine 5'-monophosphate in the absence of NAD.
[5]
CommentsCHARACTERIZATION
Medline ID95283610
PubMed ID7763314
JournalBiochem Pharmacol
Year1995
Volume49
Pages1323-9
AuthorsHager PW, Collart FR, Huberman E, Mitchell BS
TitleRecombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding.
Related UniProtKBP12268
[6]
CommentsCHARACTERIZATION
Medline ID96046660
PubMed ID7577983
JournalBiochemistry
Year1995
Volume34
Pages13889-94
AuthorsHuete-Perez JA, Wu JC, Whitby FG, Wang CC
TitleIdentification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus.
Related UniProtKBP50097
[7]
PubMed ID7562914
JournalJ Med Chem
Year1995
Volume38
Pages3829-37
AuthorsFranchetti P, Cappellacci L, Grifantini M, Barzi A, Nocentini G, Yang H, O'Connor A, Jayaram HN, Carrell C, Goldstein BM
TitleFuranfurin and thiophenfurin: two novel tiazofurin analogues. Synthesis, structure, antitumor activity, and interactions with inosine monophosphate dehydrogenase.
[8]
PubMed ID8749858
JournalProteins
Year1995
Volume23
Pages598-603
AuthorsWhitby FG, Huete-Perez J, Luecke H, Wang CC
TitlePreliminary X-ray crystallographic analysis of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase.
[9]
PubMed ID8681386
JournalCell
Year1996
Volume85
Pages921-30
AuthorsSintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP
TitleStructure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid.
Related PDB1jr1
[10]
PubMed ID8702630
JournalJ Biol Chem
Year1996
Volume271
Pages19421-7
AuthorsNimmesgern E, Fox T, Fleming MA, Thomson JA
TitleConformational changes and stabilization of inosine 5'-monophosphate dehydrogenase associated with ligand binding and inhibition by mycophenolic acid.
[11]
PubMed ID9434751
JournalArch Biochem Biophys
Year1997
Volume348
Pages378-82
AuthorsXiang B, Markham GD
TitleProbing the mechanism of inosine monophosphate dehydrogenase with kinetic isotope effects and NMR determination of the hydride transfer stereospecificity.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID97419130
PubMed ID9271497
JournalBiochemistry
Year1997
Volume36
Pages10666-74
AuthorsWhitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC
TitleCrystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex.
Related PDB1ak5
Related UniProtKBP50097
[13]
PubMed ID9371085
JournalExp Parasitol
Year1997
Volume87
Pages203-11
AuthorsLuecke H, Prosise GL, Whitby FG
TitleTritrichomonas foetus: a strategy for structure-based inhibitor design of a protozoan inosine-5'-monophosphate dehydrogenase.
[14]
PubMed ID9171883
JournalJ Med Chem
Year1997
Volume40
Pages1731-7
AuthorsFranchetti P, Cappellacci L, Sheikha GA, Jayaram HN, Gurudutt VV, Sint T, Schneider BP, Jones WD, Goldstein BM, Perra G, De Montis A, Loi AG, La Colla P, Grifantini M
TitleSynthesis, structure, and antiproliferative activity of selenophenfurin, an inosine 5'-monophosphate dehydrogenase inhibitor analogue of selenazofurin.
[15]
PubMed ID9585576
JournalBiochemistry
Year1998
Volume37
Pages7608-16
AuthorsSchalk-Hihi C, Zhang YZ, Markham GD
TitleThe conformation of NADH bound to inosine 5'-monophosphate dehydrogenase determined by transferred nuclear Overhauser effect spectroscopy.
[16]
PubMed ID10194364
JournalBiochemistry
Year1999
Volume38
Pages4433-40
AuthorsMarkham GD, Bock CL, Schalk-Hihi C
TitleAcid-base catalysis in the chemical mechanism of inosine monophosphate dehydrogenase.
[17]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID99218077
PubMed ID10200156
JournalBiochemistry
Year1999
Volume38
Pages4691-700
AuthorsZhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR
TitleCharacteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.
Related PDB1zfj
Related UniProtKBP0C0H6
[18]
PubMed ID10390598
JournalCurr Med Chem
Year1999
Volume6
Pages519-36
AuthorsGoldstein BM, Colby TD
TitleIMP dehydrogenase : structural aspects of inhibitor binding.
[19]
PubMed ID10390604
JournalCurr Med Chem
Year1999
Volume6
Pages615-28
AuthorsMinakawa N, Matsuda A
TitleMechanism-based design of inosine 5-monophosphate dehydrogenase inhibitors: synthesis and biological activities of 5-ethynyl-1-beta-D-ribofuranosylimidazole-4-carboxamide (EICAR) and its derivatives.
[20]
CommentsX-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
Medline ID99199217
PubMed ID10097070
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages3531-6
AuthorsColby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM
TitleCrystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design.
Related PDB1b3o
Related UniProtKBP12268
[21]
PubMed ID10545277
JournalProtein Expr Purif
Year1999
Volume17
Pages282-9
AuthorsNimmesgern E, Black J, Futer O, Fulghum JR, Chambers SP, Brummel CL, Raybuck SA, Sintchak MD
TitleBiochemical analysis of the modular enzyme inosine 5'-monophosphate dehydrogenase.
[22]
PubMed ID10933797
JournalBiochemistry
Year2000
Volume39
Pages9804-10
AuthorsKerr KM, Digits JA, Kuperwasser N, Hedstrom L
TitleAsp338 controls hydride transfer in Escherichia coli IMP dehydrogenase.
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID20222989
PubMed ID10758003
JournalBiochemistry
Year2000
Volume39
Pages4533-42
AuthorsMcMillan FM, Cahoon M, White A, Hedstrom L, Petsko GA, Ringe D
TitleCrystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6.
Related PDB1eep
Related UniProtKBP49058
[24]
PubMed ID10930578
JournalFEBS Lett
Year2000
Volume478
Pages253-9
AuthorsIngley E, Hemmings BA
TitlePKB/Akt interacts with inosine-5' monophosphate dehydrogenase through its pleckstrin homology domain.
[25]
CommentsX-ray crystallography
PubMed ID12403633
JournalBiochemistry
Year2002
Volume41
Pages13309-17
AuthorsGan L, Petsko GA, Hedstrom L
TitleCrystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis.
Related PDB1lrt
[26]
PubMed ID11825606
JournalBiochim Biophys Acta
Year2002
Volume1594
Pages27-39
AuthorsFuter O, Sintchak MD, Caron PR, Nimmesgern E, DeCenzo MT, Livingston DJ, Raybuck SA
TitleA mutational analysis of the active site of human type II inosine 5'-monophosphate dehydrogenase.
[27]
PubMed ID11965381
JournalBioorg Med Chem Lett
Year2002
Volume12
Pages1323-6
AuthorsGu HH, Iwanowicz EJ, Guo J, Watterson SH, Shen Z, Pitts WJ, Dhar TG, Fleener CA, Rouleau K, Sherbina NZ, Witmer M, Tredup J, Hollenbaugh D
TitleNovel diamide-based inhibitors of IMPDH.
[28]
PubMed ID12270168
JournalBioorg Med Chem Lett
Year2002
Volume12
Pages2879-82
AuthorsWatterson SH, Liu C, Dhar TG, Gu HH, Pitts WJ, Barrish JC, Fleener CA, Rouleau K, Sherbina NZ, Hollenbaugh DL, Iwanowicz EJ
TitleNovel amide-based inhibitors of inosine 5'-monophosphate dehydrogenase.
[29]
CommentsX-ray crystallography
PubMed ID12235158
JournalJ Biol Chem
Year2002
Volume277
Pages50654-9
AuthorsProsise GL, Wu JZ, Luecke H
TitleCrystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site.
Related PDB1me7,1me8
[30]
CommentsX-ray crystallography
PubMed ID12549902
JournalBiochemistry
Year2003
Volume42
Pages857-63
AuthorsGan L, Seyedsayamdost MR, Shuto S, Matsuda A, Petsko GA, Hedstrom L
TitleThe immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase.
Related PDB1pvn,1mwf
[31]
PubMed ID12565968
JournalBioorg Med Chem Lett
Year2003
Volume13
Pages543-6
AuthorsWatterson SH, Carlsen M, Dhar TG, Shen Z, Pitts WJ, Guo J, Gu HH, Norris D, Chorba J, Chen P, Cheney D, Witmer M, Fleener CA, Rouleau K, Townsend R, Hollenbaugh DL, Iwanowicz EJ
TitleNovel inhibitors of IMPDH: a highly potent and selective quinolone-based series.
[32]
CommentsX-ray crystallography
PubMed ID12559919
JournalJ Mol Biol
Year2003
Volume326
Pages517-27
AuthorsProsise GL, Luecke H
TitleCrystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism.
Related PDB1me9,1meh,1mei,1mew

comments
Although this enzyme binds potassium ion, and catalyzes potassium-dependent reaction, the role of the ion in catalysis has not been elucidated.
According to the literature, this enzyme catalyzes several reactions as follows:
(A) Addition of Cysteine residue to IMP:
(B) Hydride transfer from C2 atom of Intermediate(IMP-Cys) to NAD:
(C) Addition of water to C2 atom of the intermediate (hydration):
(D) Elimination of Cysteine residue from the intermediate:
(E) Isomerization (shift of double-bond position):

createdupdated
2005-01-042009-09-30


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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