1.1.1.205: IMP dehydrogenase

This is an abbreviated version, for detailed information about IMP dehydrogenase, go to the full flat file.

Reaction

IMP
+
NAD+
+
H2O
=
XMP
+
NADH
+
H+

Synonyms

dehydrogenase, inosinate, EC 1.2.1.14, guaB2, IMD2, IMD3, IMD4, IMP dehydrogenase, IMP DH, IMP oxidoreductase, IMP-DH, IMP:NAD oxidoreductase, IMP:NAD+ oxidoreductase, IMPD, IMPDH, IMPDH II, IMPDH-1, IMPDH-B, IMPDH-S, IMPDH1, IMPDH2, inosinate dehydrogenase, inosine 5' monophosphate dehydrogenase, inosine 5'-monophosphate dehydrogenase, inosine 5'-monophosphate dehydrogenase 2, inosine 5'-phosphate dehydrogenase, inosine 5-monophosphate dehydrogenase, inosine 5-monophosphate dehydrogenase type I, inosine 5 -monophosphate dehydrogenase, inosine monophosphate dehydrogenase, inosine monophosphate oxidoreductase, inosine-5'-monophosphate dehydrogenase, inosine-5'-phosphate dehydrogenase, inosinic acid 5-monophosphate dehydrogenase, inosinic acid dehydrogenase, mpaF, Raspberry protein, SOI12, Superoxide-inducible protein 12, type 1 inosine monophosphate, type 2 inosine monophosphate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.205 IMP dehydrogenase

Crystallization

Crystallization on EC 1.1.1.205 - IMP dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in a phosphate ion-bound form and in complex with its substrate, inosine 5'-monophosphate, and product, xanthosine 5'-monophosphate, to 2.38-2.65 A resolution. The enzyme monomer has a typical two-domain structure, the catalytic domain, which is a TIM barrel, and the CBS domain. In all structures, each monomer contains a ligand bound in the active site, i.e.phosphate anion in the apo structure and IMP and XMP in the substrate and product-bound structures, respectively. In all the structures, the CBS domains are partially disordered
at 2.4 A resolution
-
in complex with sulfate, at 2.4 A resolution
-
in complex with inosine 5'-phosphate and mycophenolic acid at 2.6 A resolution
-
in complex with xanthosine 5'-phosphate, inhibitor mycophenolic acid and K+, at 2.6 A resolution
-
in complex with NAD+ and IMP, to 2.5 A resolution. Space group I422
hanging drop vapour diffusion method, to 3.2 A resolution, space group P21212. In complex with inhibitor N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide, to 2.8 A resolution. The thiazole ring of the inhibitor stacks against the purine ring of IMP perpendicularly, and the remainder of the inhibtor extends across the subunit interface into a pocket in the adjacent monomer, where the bromoaniline moiety interacts with Tyr358 from the adjacent subunit. This residue forms a hydrogen-bonding network involving Glu329, Ser354, Thr221, and possibly the amide nitrogen of N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide. Residues Ser22, Pro26, Gly357 of the adjacent subunit and Ala165 form the remainder of the inhibitor binding pocket. With the exception of Thr221, all of these residues are different in human IMPDHs
-
enzyme type II complexed with 6-Cl-IMP and selenazole-4-carboxamide adenine dinucleotide, no method mentioned
modeling of complex with inhibitor 9-(5-O-[hydroxy[([hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl]oxy)methyl]phosphoryl]-b-L-ribofuranosyl)-9H-purin-6-amine; modeling of complex with inhibitor 9-(5-O-[hydroxy[([hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl]oxy)methyl]phosphoryl]-b-L-ribofuranosyl)-9H-purin-6-amine
molecular modeling of type II enzyme in complex with inhibitor 1_1_1.205_2.3
-
type 1 in complex with inhibitor 6-Cl-inosine 5'-phosphate, at 2.6 A resolution, type 2 in complex with inhibitor 6-Cl-inosine 5'-phosphate and SAD or NAD, at 2.9 A resolution, and with inhibitors ribavirin-monophosphate and C2-mycophenolic adenine nucleotide, at 2.65 A resolution
-
type II isoform, in complex with 6-chloropurine riboside 5'-monophosphate and selenazole-4-carboxyamide-adenine dinucleotide at 2.9 A resolution, in complex with ribavirin monophosphate and phosphonic acidmono-[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-isobenzofuran-5-yl)-ethyl] ester at 2.65 resolution, in complex with with 6-chloropurine riboside 5'-monophosphate and NAD+ at 2.9 A resolution; type I isoform, in complex with 6-chloropurine riboside 5'-monophosphate at 2.5 A resolution
-
modeling of enzyme in complex with eicosadienoic acid. Eicosadienoic acid binds to residue C331 in the active site
-
modeling of complex with inhibitor 9-(5-O-[hydroxy[([hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl]oxy)methyl]phosphoryl]-b-L-ribofuranosyl)-9H-purin-6-amine
-
to 2.25 A resolution. Strucuture is a homotetramer of subunits dominated by a (beta/alpha)8-barrel fold. The cystathionine beta-synthase domains, residues 92-204, are not present in the model owing to disorder. A loop that creates part of the active site is composed of residues 297-315, links alpha8 and beta9 and carries the catalytic Cys304
in complex with xanthosine 5'-phosphate at 2.1 A resolution
-
in complex with inosine 5'-phosphate at 1.9 A resolution
-
in complex with inosine 5'-phosphate, at 1.9 A resolution
-
tetramer structure of IMPDH shows square planar geometry
-
vapor diffusion method using hanging drops
-
at 2.18 A resolution
-
analysis of crystal structures. The Cys319 loop has different conformations during the dehydrogenase and hydrolase reactions as suggested by the crystal structures. The structure of the Cys319 loop modulates the closure of themobile flap. This conformational change converts the enzyme from a dehydrogenase into hydrolase, suggesting that the conformation of the Cys319 loop may gate the catalytic cycle
-
at 2.3 A resolution, in complex with inosine 5'-phosphate and beta-methylene-thiazole-4-carboxyamide-adenine dinucleotide at 2.2 A resolution, in complex with xanthosine 5'-phosphate and NAD+ at 2.15 A resolution, in complex with xanthosine 5'-phosphate and mycophenolic acid at 2.2 A resolution, in complex with RVP and mycophenolic acid at 2.15 A resolution, in complex with 4-carbamoyl-1-beta-D-ribofuranosylimidazolium-5-olate-5'-phosphate at 2.0 A resolution
-
no method mentioned
-
purified recombinant full-length enzyme and alphabeta core domain in complex with inosine 5'-phosphate and beta-methylene-thiazole-4-carboxamide adenine dinucleotide, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
-
wild-type at 2.3 A resolution, in complex with xanthosine 5'-phosphate, at 2.6 A resolution, in complex with inhibitor ribavirin-monophosphate, at 1.9 A resolution, in complex with inhibitors ribavirin-monophosphate and mycophenolic acid, at 2.5 A resolution, in complex with inosine 5'-phosphate, at 2.2 A resolution, in complex with inosine 5'-phosphate and inhibitor mycophenolic acid, at 1.95 A resolution, in complex with xanthosine 5'-phosphate and inhibitor mycophenolic acid, at 2.2 A resolution, in complex with xanthosine 5'-phosphate and NAD+, at 2.15 A resolution. Mutant DELTA(101-226) in complex with inosine 5'-phosphate and inhibitor beta-CH2-tiazofurin adenine dinucletoide, at 2.2 A resolution or in complex with inhibitor mizoribine monophosphate, at 2 A resolution
-