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Literature summary for 1.1.1.205 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
Search for more literature for 1.1.1.205

Cloned(Commentary)

Cloned (Comment) Organism
-
 Cryptosporidium parvum

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum
-
-
-
Homo sapiens
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
-
 Homo sapiens xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
 ?
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
-
 Cryptosporidium parvum xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
 ?
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+
-
 ?
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

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

Turnover Number [1/s]

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

Cofactor

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