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
IMPDH IMPD EC 1.1.1.205 |
NP_047003.1
(Protein)
NC_001903.1 (DNA/RNA sequence) |
PF00478
(IMPDH)
[Graphical View] |
| Q9X168 |
|
Inosine-5''-monophosphate dehydrogenase
|
NP_229148.1
(Protein)
NC_000853.1 (DNA/RNA sequence) |
PF00571
(CBS)
PF00478 (IMPDH) [Graphical View] |
| P0C0H6 |
Inosine-5''-monophosphate dehydrogenase
|
IMP dehydrogenase
IMPDH IMPD EC 1.1.1.205 |
PF00571
(CBS)
PF00478 (IMPDH) [Graphical View] |
|
| P50097 |
Inosine-5''-monophosphate dehydrogenase
|
IMP dehydrogenase
IMPDH IMPD EC 1.1.1.205 |
PF00571
(CBS)
PF00478 (IMPDH) [Graphical View] |
|
| P12269 |
Inosine-5''-monophosphate dehydrogenase 2
|
IMP dehydrogenase 2
EC 1.1.1.205 IMPDH-II IMPD 2 |
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
EC 1.1.1.205 IMPDH-I IMPD 1 |
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
EC 1.1.1.205 IMPDH-II IMPD 2 |
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. |
|---|---|---|
| MAP00230 | Purine metabolism | |
| MAP00983 | Drug metabolism - other enzymes |
| 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 29103 |
17202 17202 |
15846 15846 |
15377 15377 |
15652 15652 |
16908 16908 |
||||||
| PubChem |
813 813 |
8582 8582 |
5893 5893 |
22247451 962 22247451 962 |
73323 73323 |
439153 439153 |
||||||
| 1eepA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1eepB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1vrdA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1vrdB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1zfjA |
|
|
|
|
|
Unbound | Bound:IMP | Unbound | Unbound | Unbound | Unbound | |
| 1ak5A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1lrtA |
|
|
|
|
|
Unbound | Bound:IMP | Analogue:TAD | Unbound | Unbound | Unbound | |
| 1lrtB |
|
|
|
|
|
Unbound | Bound:IMP | Analogue:TAD | Unbound | Unbound | Unbound | |
| 1lrtC |
|
|
|
|
|
Unbound | Bound:IMP | Analogue:TAD | Unbound | Unbound | Unbound | |
| 1lrtD |
|
|
|
|
|
Unbound | Bound:IMP | Analogue:TAD | Unbound | Unbound | Unbound | |
| 1me7A |
|
|
|
|
|
Analogue:_NA | Analogue:RVP | Analogue:MOA | Unbound | Unbound | Unbound | |
| 1me8A |
|
|
|
|
|
Analogue:_NA | Analogue:RVP | Unbound | Unbound | Unbound | Unbound | |
| 1me9A |
|
|
|
|
|
Unbound | Bound:IMP | Unbound | Unbound | Unbound | Unbound | |
| 1mehA |
|
|
|
|
|
Unbound | Bound:IMP | Analogue:MOA | Unbound | Unbound | Unbound | |
| 1meiA |
|
|
|
|
|
Unbound | Unbound | Analogue:MOA | Bound:XMP | Unbound | Unbound | |
| 1mewA |
|
|
|
|
|
Unbound | Unbound | Bound:NAD | Bound:XMP | Unbound | Unbound | |
| 1mwfA |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1mwfB |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1mwfC |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1mwfD |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1pvnA |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1pvnB |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1pvnC |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1pvnD |
|
|
|
|
|
Bound:__K | Analogue:MZP | Unbound | Unbound | Unbound | Unbound | |
| 1jr1A |
|
|
|
|
|
Bound:__K | Unbound | Analogue:MOA | Unbound | Unbound | Intermediate-bound:CYS_331-IMP | |
| 1jr1B |
|
|
|
|
|
Bound:__K | Bound:IMP | Analogue:MOA | Unbound | Unbound | Unbound | |
| 1jcnA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CYS_331-CPR | |
| 1jcnB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CYS_331-CPR | |
| 1b3oA |
|
|
|
|
|
Unbound | Analogue:CPR | Analogue:SAE | Unbound | Unbound | Unbound | |
| 1b3oB |
|
|
|
|
|
Unbound | Unbound | Analogue:SAE | Unbound | Unbound | Intermediate-analogue:CYS_331-CPR | |
| 1nfbA |
|
|
|
|
|
Unbound | Unbound | Bound:NAD | Unbound | Unbound | Intermediate-analogue:CYS_331-CPR | |
| 1nfbB |
|
|
|
|
|
Unbound | Unbound | Bound:NAD | Unbound | Unbound | Intermediate-analogue:CYS_331-CPR | |
| 1nf7A |
|
|
|
|
|
Bound:__K | Analogue:RVP | Analogue:MYD | Unbound | Unbound | Unbound | |
| 1nf7B |
|
|
|
|
|
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 |
|
|
|
|
|
ASP 172;ASN 201;LYS 220;CYS 229;THR 231 | GLY 224;GLY 226(Potassium binding) | |||
| 1eepB |
|
|
|
|
|
ASP 172;ASN 201;LYS 220;CYS 229;THR 231 | GLY 224;GLY 226(Potassium binding) | |||
| 1vrdA |
|
|
|
|
|
ASP 244;ASN 273;LYS 292;CYS 301;THR 303 | GLY 296;GLY 298(Potassium binding) | |||
| 1vrdB |
|
|
|
|
|
ASP 244;ASN 273;LYS 292;CYS 301;THR 303 | GLY 296;GLY 298(Potassium binding) | |||
| 1zfjA |
|
|
|
|
|
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 |
|
|
|
|
|
ASP 261;ASN 291;LYS 310; ; | ; | invisible 314-327 | ||
| 1lrtA |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319; | GLY 314;GLY 316(Potassium binding) | invisible 320-322 | ||
| 1lrtB |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319; | GLY 314;GLY 316(Potassium binding) | invisible 320-322 | ||
| 1lrtC |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319; | GLY 314;GLY 316(Potassium binding) | invisible 320-322 | ||
| 1lrtD |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1me7A |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1me8A |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;;THR 321 | GLY 314;GLY 316(Potassium binding) | CSO 319(S-hydroxylated) | ||
| 1me9A |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;;THR 321 | GLY 314;GLY 316(Potassium binding) | CSO 319(S-hydroxylated) | ||
| 1mehA |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;;THR 321 | GLY 314;GLY 316(Potassium binding) | CSO 319(S-hydroxylated) | ||
| 1meiA |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1mewA |
|
|
|
|
|
ASP 261;ASN 291; ; | GLY 314;GLY 316(Potassium binding) | invisible 318-321 | ||
| 1mwfA |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1mwfB |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1mwfC |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1mwfD |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1pvnA |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1pvnB |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1pvnC |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1pvnD |
|
|
|
|
|
ASP 261;ASN 291;LYS 310;CYS 319;THR 321 | GLY 314;GLY 316(Potassium binding) | |||
| 1jr1A |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1jr1B |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1jcnA |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1jcnB |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1b3oA |
|
|
|
|
|
ASP 274;ASN 303;ARG 322; ; | GLY 326; (Potassium binding) | invisible 110-231/328-340/401-448 | ||
| 1b3oB |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | invisible 160-177/401-448 | ||
| 1nfbA |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1nfbB |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1nf7A |
|
|
|
|
|
ASP 274;ASN 303;ARG 322;CYS 331;THR 333 | GLY 326;GLY 328(Potassium binding) | |||
| 1nf7B |
|
|
|
|
|
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. |
| 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. |
| 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. |
| 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, |
| 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, |
| Related PDB | 1me9 1meh 1mei 1mew |
| Related UniProtKB | |
| Comments |
|---|
|
Although this enzyme binds potassium ion, According to the literature, (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 |