DB code: S00215

CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
E.C. 1.1.1.205
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.20.20.70 : TIM Barrel S00217 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P49058 Inosine-5''-monophosphate dehydrogenase
IMP dehydrogenase
IMPD
IMPDH
EC 1.1.1.205
NP_047003.1 (Protein)
NC_001903.1 (DNA/RNA sequence)
PF00478 (IMPDH)
[Graphical View]
Q9X168 Inosine-5''-monophosphate dehydrogenase
IMP dehydrogenase
IMPD
IMPDH
EC 1.1.1.205
NP_229148.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]
P0C0H6 Inosine-5''-monophosphate dehydrogenase
IMP dehydrogenase
IMPD
IMPDH
EC 1.1.1.205
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]
P50097 Inosine-5''-monophosphate dehydrogenase
IMP dehydrogenase
IMPD
IMPDH
EC 1.1.1.205
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]
P12269 Inosine-5''-monophosphate dehydrogenase 2
IMP dehydrogenase 2
IMPD 2
IMPDH 2
EC 1.1.1.205
IMPDH-II
NP_001233751.1 (Protein)
NM_001246822.1 (DNA/RNA sequence)
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]
P20839 Inosine-5''-monophosphate dehydrogenase 1
IMP dehydrogenase 1
IMPD 1
IMPDH 1
EC 1.1.1.205
IMPDH-I
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)
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]
P12268 Inosine-5''-monophosphate dehydrogenase 2
IMP dehydrogenase 2
IMPD 2
IMPDH 2
EC 1.1.1.205
IMPDH-II
NP_000875.2 (Protein)
NM_000884.2 (DNA/RNA sequence)
PF00571 (CBS)
PF00478 (IMPDH)
[Graphical View]

KEGG enzyme name
IMP dehydrogenase
inosine-5'-phosphate dehydrogenase
inosinic acid dehydrogenase
inosinate dehydrogenase
inosine 5'-monophosphate dehydrogenase
inosine monophosphate dehydrogenase
IMP oxidoreductase
inosine monophosphate oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P49058 IMDH_BORBU Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH.
Q9X168 Q9X168_THEMA Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH.
P0C0H6 IMDH_STRPY Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH. Homotetramer.
P50097 IMDH_TRIFO Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH. Homotetramer.
P12269 IMDH2_CRIGR Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH. Homotetramer. Potassium.
P20839 IMDH1_HUMAN Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH. Homotetramer. Potassium (By similarity).
P12268 IMDH2_HUMAN Inosine 5''-phosphate + NAD(+) + H(2)O = xanthosine 5''-phosphate + NADH. Homotetramer. Potassium.

KEGG Pathways
Map code Pathways E.C.
MAP00983 Drug metabolism - other enzymes
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00238 C00130 C00003 C00001 C00655 C00004
E.C. (covalently bound)
Compound Potassium Inosine 5'-phosphate NAD+ H2O Xanthosine 5'-phosphate NADH Enzyme-Cys-IMP
Type univalent metal (Na+, K+) amide group,nucleotide amide group,amine group,nucleotide H2O amide group,nucleotide amide group,amine group,nucleotide
ChEBI 29103
17202
15846
15377
15652
16908
PubChem 813
8582
5893
22247451
962
73323
439153
1eepA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1eepB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1vrdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1vrdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zfjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Unbound Unbound Unbound Unbound
1ak5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1lrtA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Analogue:TAD Unbound Unbound Unbound
1lrtB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Analogue:TAD Unbound Unbound Unbound
1lrtC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Analogue:TAD Unbound Unbound Unbound
1lrtD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Analogue:TAD Unbound Unbound Unbound
1me7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_NA Analogue:RVP Analogue:MOA Unbound Unbound Unbound
1me8A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_NA Analogue:RVP Unbound Unbound Unbound Unbound
1me9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Unbound Unbound Unbound Unbound
1mehA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IMP Analogue:MOA Unbound Unbound Unbound
1meiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:MOA Bound:XMP Unbound Unbound
1mewA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAD Bound:XMP Unbound Unbound
1mwfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1mwfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1mwfC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1mwfD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1pvnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1pvnB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1pvnC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1pvnD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:MZP Unbound Unbound Unbound Unbound
1jr1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Unbound Analogue:MOA Unbound Unbound Intermediate-bound:CYS_331-IMP
1jr1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Bound:IMP Analogue:MOA Unbound Unbound Unbound
1jcnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:CYS_331-CPR
1jcnB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:CYS_331-CPR
1b3oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:CPR Analogue:SAE Unbound Unbound Unbound
1b3oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:SAE Unbound Unbound Intermediate-analogue:CYS_331-CPR
1nfbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAD Unbound Unbound Intermediate-analogue:CYS_331-CPR
1nfbB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAD Unbound Unbound Intermediate-analogue:CYS_331-CPR
1nf7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:RVP Analogue:MYD Unbound Unbound Unbound
1nf7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:__K Analogue:RVP Analogue:MYD Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P12268, P49058, P0C0H6, P50097 & PDB;1zfj

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eepA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 172;ASN 201;LYS 220;CYS 229;THR 231 GLY 224;GLY 226(Potassium binding)
1eepB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 172;ASN 201;LYS 220;CYS 229;THR 231 GLY 224;GLY 226(Potassium binding)
1vrdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 244;ASN 273;LYS 292;CYS 301;THR 303 GLY 296;GLY 298(Potassium binding)
1vrdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 244;ASN 273;LYS 292;CYS 301;THR 303 GLY 296;GLY 298(Potassium binding)
1zfjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 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)
1ak5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310; ; ; invisible 314-327
1lrtA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319; GLY 314;GLY 316(Potassium binding) invisible 320-322
1lrtB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319; GLY 314;GLY 316(Potassium binding) invisible 320-322
1lrtC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319; GLY 314;GLY 316(Potassium binding) invisible 320-322
1lrtD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1me7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1me8A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;;THR 321 GLY 314;GLY 316(Potassium binding) CSO 319(S-hydroxylated)
1me9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;;THR 321 GLY 314;GLY 316(Potassium binding) CSO 319(S-hydroxylated)
1mehA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;;THR 321 GLY 314;GLY 316(Potassium binding) CSO 319(S-hydroxylated)
1meiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1mewA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291; ; GLY 314;GLY 316(Potassium binding) invisible 318-321
1mwfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1mwfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1mwfC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1mwfD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1pvnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1pvnB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1pvnC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1pvnD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 261;ASN 291;LYS 310;CYS 319;THR 321 GLY 314;GLY 316(Potassium binding)
1jr1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1jr1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1jcnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1jcnB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1b3oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322; ; GLY 326; (Potassium binding) invisible 110-231/328-340/401-448
1b3oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding) invisible 160-177/401-448
1nfbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1nfbB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1nf7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)
1nf7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 274;ASN 303;ARG 322;CYS 331;THR 333 GLY 326;GLY 328(Potassium binding)

References for Catalytic Mechanism
References Sections No. 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
[1]
Resource
Comments
Medline ID
PubMed ID 1967649
Journal J Med Chem
Year 1990
Volume 33
Pages 572-6
Authors Riley TA, Larson SB, Avery TL, Finch RA, Robins RK
Title 1,2,4-Diazaphosphole nucleosides. Synthesis, structure, and antitumor activity of nucleosides with a lambda 3 phosphorus atom.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1357174
Journal J Med Chem
Year 1992
Volume 35
Pages 3560-7
Authors Li H, Goldstein BM
Title Carboxamide group conformation in the nicotinamide and thiazole-4-carboxamide rings: implications for enzyme binding.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7903306
Journal J Biol Chem
Year 1993
Volume 268
Pages 27286-90
Authors Carr SF, Papp E, Wu JC, Natsumeda Y
Title Characterization of human type I and type II IMP dehydrogenases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7906542
Journal Biochemistry
Year 1994
Volume 33
Pages 1753-9
Authors Antonino LC, Wu JC
Title Human IMP dehydrogenase catalyzes the dehalogenation of 2-fluoro- and 2-chloroinosine 5'-monophosphate in the absence of NAD.
Related PDB
Related UniProtKB
[5]
Resource
Comments CHARACTERIZATION
Medline ID 95283610
PubMed ID 7763314
Journal Biochem Pharmacol
Year 1995
Volume 49
Pages 1323-9
Authors Hager PW, Collart FR, Huberman E, Mitchell BS
Title Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding.
Related PDB
Related UniProtKB P12268
[6]
Resource
Comments CHARACTERIZATION
Medline ID 96046660
PubMed ID 7577983
Journal Biochemistry
Year 1995
Volume 34
Pages 13889-94
Authors Huete-Perez JA, Wu JC, Whitby FG, Wang CC
Title Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus.
Related PDB
Related UniProtKB P50097
[7]
Resource
Comments
Medline ID
PubMed ID 7562914
Journal J Med Chem
Year 1995
Volume 38
Pages 3829-37
Authors Franchetti P, Cappellacci L, Grifantini M, Barzi A, Nocentini G, Yang H, O'Connor A, Jayaram HN, Carrell C, Goldstein BM
Title Furanfurin and thiophenfurin: two novel tiazofurin analogues. Synthesis, structure, antitumor activity, and interactions with inosine monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8749858
Journal Proteins
Year 1995
Volume 23
Pages 598-603
Authors Whitby FG, Huete-Perez J, Luecke H, Wang CC
Title Preliminary X-ray crystallographic analysis of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8681386
Journal Cell
Year 1996
Volume 85
Pages 921-30
Authors Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP
Title Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid.
Related PDB 1jr1
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8702630
Journal J Biol Chem
Year 1996
Volume 271
Pages 19421-7
Authors Nimmesgern E, Fox T, Fleming MA, Thomson JA
Title Conformational changes and stabilization of inosine 5'-monophosphate dehydrogenase associated with ligand binding and inhibition by mycophenolic acid.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9434751
Journal Arch Biochem Biophys
Year 1997
Volume 348
Pages 378-82
Authors Xiang B, Markham GD
Title Probing the mechanism of inosine monophosphate dehydrogenase with kinetic isotope effects and NMR determination of the hydride transfer stereospecificity.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 97419130
PubMed ID 9271497
Journal Biochemistry
Year 1997
Volume 36
Pages 10666-74
Authors Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC
Title Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex.
Related PDB 1ak5
Related UniProtKB P50097
[13]
Resource
Comments
Medline ID
PubMed ID 9371085
Journal Exp Parasitol
Year 1997
Volume 87
Pages 203-11
Authors Luecke H, Prosise GL, Whitby FG
Title Tritrichomonas foetus: a strategy for structure-based inhibitor design of a protozoan inosine-5'-monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9171883
Journal J Med Chem
Year 1997
Volume 40
Pages 1731-7
Authors Franchetti 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
Title Synthesis, structure, and antiproliferative activity of selenophenfurin, an inosine 5'-monophosphate dehydrogenase inhibitor analogue of selenazofurin.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9585576
Journal Biochemistry
Year 1998
Volume 37
Pages 7608-16
Authors Schalk-Hihi C, Zhang YZ, Markham GD
Title The conformation of NADH bound to inosine 5'-monophosphate dehydrogenase determined by transferred nuclear Overhauser effect spectroscopy.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10194364
Journal Biochemistry
Year 1999
Volume 38
Pages 4433-40
Authors Markham GD, Bock CL, Schalk-Hihi C
Title Acid-base catalysis in the chemical mechanism of inosine monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID 99218077
PubMed ID 10200156
Journal Biochemistry
Year 1999
Volume 38
Pages 4691-700
Authors Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR
Title Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.
Related PDB 1zfj
Related UniProtKB P0C0H6
[18]
Resource
Comments
Medline ID
PubMed ID 10390598
Journal Curr Med Chem
Year 1999
Volume 6
Pages 519-36
Authors Goldstein BM, Colby TD
Title IMP dehydrogenase : structural aspects of inhibitor binding.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10390604
Journal Curr Med Chem
Year 1999
Volume 6
Pages 615-28
Authors Minakawa N, Matsuda A
Title Mechanism-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.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
Medline ID 99199217
PubMed ID 10097070
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 3531-6
Authors Colby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM
Title Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design.
Related PDB 1b3o
Related UniProtKB P12268
[21]
Resource
Comments
Medline ID
PubMed ID 10545277
Journal Protein Expr Purif
Year 1999
Volume 17
Pages 282-9
Authors Nimmesgern E, Black J, Futer O, Fulghum JR, Chambers SP, Brummel CL, Raybuck SA, Sintchak MD
Title Biochemical analysis of the modular enzyme inosine 5'-monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 10933797
Journal Biochemistry
Year 2000
Volume 39
Pages 9804-10
Authors Kerr KM, Digits JA, Kuperwasser N, Hedstrom L
Title Asp338 controls hydride transfer in Escherichia coli IMP dehydrogenase.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID 20222989
PubMed ID 10758003
Journal Biochemistry
Year 2000
Volume 39
Pages 4533-42
Authors McMillan FM, Cahoon M, White A, Hedstrom L, Petsko GA, Ringe D
Title Crystal 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 PDB 1eep
Related UniProtKB P49058
[24]
Resource
Comments
Medline ID
PubMed ID 10930578
Journal FEBS Lett
Year 2000
Volume 478
Pages 253-9
Authors Ingley E, Hemmings BA
Title PKB/Akt interacts with inosine-5' monophosphate dehydrogenase through its pleckstrin homology domain.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12403633
Journal Biochemistry
Year 2002
Volume 41
Pages 13309-17
Authors Gan L, Petsko GA, Hedstrom L
Title Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis.
Related PDB 1lrt
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11825606
Journal Biochim Biophys Acta
Year 2002
Volume 1594
Pages 27-39
Authors Futer O, Sintchak MD, Caron PR, Nimmesgern E, DeCenzo MT, Livingston DJ, Raybuck SA
Title A mutational analysis of the active site of human type II inosine 5'-monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 11965381
Journal Bioorg Med Chem Lett
Year 2002
Volume 12
Pages 1323-6
Authors Gu 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
Title Novel diamide-based inhibitors of IMPDH.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 12270168
Journal Bioorg Med Chem Lett
Year 2002
Volume 12
Pages 2879-82
Authors Watterson SH, Liu C, Dhar TG, Gu HH, Pitts WJ, Barrish JC, Fleener CA, Rouleau K, Sherbina NZ, Hollenbaugh DL, Iwanowicz EJ
Title Novel amide-based inhibitors of inosine 5'-monophosphate dehydrogenase.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12235158
Journal J Biol Chem
Year 2002
Volume 277
Pages 50654-9
Authors Prosise GL, Wu JZ, Luecke H
Title Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site.
Related PDB 1me7 1me8
Related UniProtKB
[30]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12549902
Journal Biochemistry
Year 2003
Volume 42
Pages 857-63
Authors Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, Petsko GA, Hedstrom L
Title The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase.
Related PDB 1pvn 1mwf
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 12565968
Journal Bioorg Med Chem Lett
Year 2003
Volume 13
Pages 543-6
Authors Watterson 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
Title Novel inhibitors of IMPDH: a highly potent and selective quinolone-based series.
Related PDB
Related UniProtKB
[32]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12559919
Journal J Mol Biol
Year 2003
Volume 326
Pages 517-27
Authors Prosise GL, Luecke H
Title Crystal 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 PDB 1me9 1meh 1mei 1mew
Related UniProtKB

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):

Created Updated
2005-01-04 2009-09-30