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Literature summary for 1.1.1.205 extracted from

  • Hedstrom, L.; Gan, L.
    IMP dehydrogenase: structural schizophrenia and an unusual base (2006), Curr. Opin. Chem. Biol., 10, 520-525.
    View publication on PubMed

Application

Application Comment Organism
drug development the enzyme is a target for drug development in treatment of structural schizophrenia Homo sapiens

Protein Variants

Protein Variants Comment Organism
R418A site-directed mutagenesis, chemical rescue of the mutant by guanidine, methylguanidine, ethylguanidine, acteamide, and aminoguanidine, not by hydroxyurea, overview Tritrichomonas suis

Inhibitors

Inhibitors Comment Organism Structure
beta-methylene thiazole 4-carboxamide adenine dinucleotide i.e. beta-Me-TAD or CH2-TAD Homo sapiens
beta-methylene thiazole 4-carboxamide adenine dinucleotide i.e. beta-Me-TAD Tritrichomonas suis
mizoribine 5'-phosphate complexes the enzyme Tritrichomonas suis
additional information the enzyme is resistant to mizoribine 5'-phosphate due to its open dehydrogenase conformation in opposite to the bacterial enzyme which has a closed hydrolase conformation Homo sapiens
Mycophenolic acid traps the reaction intermediate E-XMP, the human enzyme is sensitive to the inhibitor due to its open dehydrogenase conformation Homo sapiens
ribavirin 5'-phosphate
-
Homo sapiens
ribavirin 5'-phosphate
-
Tritrichomonas suis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
inosine 5'-phosphate + NAD+ + H2O Homo sapiens
-
xanthosine 5'-phosphate + NADH
-
r
inosine 5'-phosphate + NAD+ + H2O Tritrichomonas suis
-
xanthosine 5'-phosphate + NADH
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Tritrichomonas suis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
IMP + NAD+ + H2O = XMP + NADH + H+ reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base Homo sapiens
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 Tritrichomonas suis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the bacterial enzyme shows low activity due to its open dehydrogenase conformation in opposite to the bacterial enzyme which has a closed hydrolase conformation Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
inosine 5'-phosphate + NAD+ + H2O
-
Homo sapiens xanthosine 5'-phosphate + NADH
-
r
inosine 5'-phosphate + NAD+ + H2O
-
Tritrichomonas suis xanthosine 5'-phosphate + NADH
-
r

Subunits

Subunits Comment Organism
tetramer the enzyme forms a homotetramer with four active sites Tritrichomonas suis
tetramer the enzyme forms a homotetramer with four active sites and an open dehydrogenase conformation Homo sapiens

Synonyms

Synonyms Comment Organism
IMPDH
-
Homo sapiens
IMPDH
-
Tritrichomonas suis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NAD+
-
Tritrichomonas suis
NADH
-
Homo sapiens
NADH
-
Tritrichomonas suis