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Information on EC 1.1.1.205 - IMP dehydrogenase
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EC Tree 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
IUBMB Comments
The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
The enzyme appears in viruses and cellular organisms
- 1.1.1.205
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mycophenolic
- purine
- guanine
- mofetil
- ribavirin
- leukemia
- tiazofurin
-
rejection
- xmp
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pharmacodynamic
-
salvage
- hypoxanthine
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cyclosporine
-
allograft
-
prodrugs
- mizoribine
- phosphoribosyltransferase
- ribonucleotide
- xanthosine
-
guanylate
- tad
- calcineurin
- dgtp
- adenylosuccinate
- 6-mercaptopurine
- dihydrofolate
-
hypoxanthine-guanine
- cryptosporidium
- tacrolimus
- thiopurine
- riboside
- azathioprine
- glucuronide
- parvum
- benzamide
- pigmentosa
- sirolimus
- 6-thioguanine
- analysis
- rbv
-
amido
- cryptosporidiosis
-
c-nucleoside
- tritrichomonas
-
enteric-coated
-
predose
- hgprt
- pharmacology
- diagnostics
- drug development
- medicine
showSynonyms
impdh, imp dehydrogenase, inosine monophosphate dehydrogenase, impdh2, impdh1, inosine 5'-monophosphate dehydrogenase, inosine-5'-monophosphate dehydrogenase, impdh ii, imp dh, inosinate dehydrogenase, more
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
IMP + NAD+ + H2O = XMP + NADH + H+
enzyme acts on the hydroxyl group of the hydrated derivative of the substrate, ordered bi-bi mechanism
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IMP + NAD+ + H2O = XMP + NADH + H+
enzyme acts on the hydroxyl group of the hydrated derivative of the substrate, ordered bi-bi mechanism
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IMP + NAD+ + H2O = XMP + NADH + H+
IMP and K+ can bind randomly to the free enzyme, while NAD+ does not react unless K+ or both K+ and IMP are present on the enzyme
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IMP + NAD+ + H2O = XMP + NADH + H+
IMP binds first, followed by NAD+, NADH dissociates from the ternary complex first, then XMP is released
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IMP + NAD+ + H2O = XMP + NADH + H+
mechanism is partially random
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IMP + NAD+ + H2O = XMP + NADH + H+
Arg418 is involved in the reaction mechanism as catalytic base
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IMP + NAD+ + H2O = XMP + NADH + H+
covalent enzyme reaction intermediate, hydrolysis of enzyme-XMP is rate-limiting and requires the adoption of the closed conformation, Arg418 is involved in the reaction mechanism as catalytic base, Thr321 is involved in both hydride transfer and hydrolysis
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base, Cys319-linked covalent enzyme intermediate E-XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
substrate binding and catalytic reaction mechanism, Cys319 is the catalytic residue, NAD+ promotes the nucleophilic attack of Cys319 on IMP
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IMP + NAD+ + H2O = XMP + NADH + H+
a steady-state ordered Bi Bi kinetic mechanism in which IMP binds first followed by NAD+, and product release is ordered. Hydride transfer appears not to be rate-limiting. The pH-rate profile indicates one deprotonated group essential for catalysis
IMP + NAD+ + H2O = XMP + NADH + H+
reaction in two steps via covalent interemediate state, the catalytic residue is Cys334
IMP + NAD+ + H2O = XMP + NADH + H+
the enzymatic mechanism of IMPDH consists two steps, a dehydrogenase and a hydrolase reaction. Upon binding of IMP and NAD+ cofactor, a thioimidate enzyme-substrate adduct, E-XMP*, is formed via a covalent bond to the catalytic C341 with concurrent production of NADH. Hydride transfer occurs to the pro-S position with the cofactor in the anti-conformation. The cofactor is released and an active site mobile flap moves into the NAD+ site and facilitates E-XMP* hydrolysis with a conserved R443 acting as a general base. The enzyme has two distinct conformations, an open form for the dehydrogenase reaction and a closed form for E-XMP* hydrolysis
IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the enzymatic mechanism of IMPDH consists two steps, a dehydrogenase and a hydrolase reaction. Upon binding of IMP and NAD+ cofactor, a thioimidate enzyme-substrate adduct, E-XMP*, is formed via a covalent bond to the catalytic C341 with concurrent production of NADH. Hydride transfer occurs to the pro-S position with the cofactor in the anti-conformation. The cofactor is released and an active site mobile flap moves into the NAD+ site and facilitates E-XMP* hydrolysis with a conserved R443 acting as a general base. The enzyme has two distinct conformations, an open form for the dehydrogenase reaction and a closed form for E-XMP* hydrolysis
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IMP + NAD+ + H2O = XMP + NADH + H+
a steady-state ordered Bi Bi kinetic mechanism in which IMP binds first followed by NAD+, and product release is ordered. Hydride transfer appears not to be rate-limiting. The pH-rate profile indicates one deprotonated group essential for catalysis
-
-
IMP + NAD+ + H2O = XMP + NADH + H+
reaction in two steps via covalent interemediate state, the catalytic residue is Cys334
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IMP + NAD+ + H2O = XMP + NADH + H+
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