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Literature summary extracted from

  • Riera, T.V.; Wang, W.; Josephine, H.R.; Hedstrom, L.
    A kinetic alignment of orthologous inosine-5-monophosphate dehydrogenases (2008), Biochemistry, 47, 8689-8696.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.205
-
 Cryptosporidium parvum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.205 0.006
-
 NAD+ pH 8.0, 25°C Homo sapiens
1.1.1.205 0.14
-
 NAD+
-
 Cryptosporidium parvum
1.1.1.205 0.19
-
 acetylpyridine adenine dinucleotide
-
 Cryptosporidium parvum

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.205 Cryptosporidium parvum
-
-
-
1.1.1.205 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.205 to more than 95% purity Cryptosporidium parvum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.205 inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
-
 Homo sapiens xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
 ?
1.1.1.205 inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
-
 Cryptosporidium parvum xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
 ?
1.1.1.205 inosine 5'-phosphate + NAD+ + H2O IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites Cryptosporidium parvum xanthosine 5'-phosphate + NADH + H+
-
 ?
1.1.1.205 inosine 5'-phosphate + NAD+ + H2O IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate* and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites Homo sapiens xanthosine 5'-phosphate + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.205 IMPDH
-
 Cryptosporidium parvum
1.1.1.205 IMPDH2
-
 Homo sapiens
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Homo sapiens
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Cryptosporidium parvum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.205 0.39
-
 NAD+ pH 8.0, 25°C Homo sapiens
1.1.1.205 2.6
-
 NAD+
-
 Cryptosporidium parvum
1.1.1.205 3
-
 acetylpyridine adenine dinucleotide
-
 Cryptosporidium parvum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.205 additional information acetylpyridine adenine dinucleotide Cryptosporidium parvum
1.1.1.205 NAD+
-
 Homo sapiens
1.1.1.205 NAD+
-
 Cryptosporidium parvum