Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Riera, T.V.; Zheng, L.; Josephine, H.R.; Min, D.; Yang, W.; Hedstrom, L.
    Allosteric activation via kinetic control: potassium accelerates a conformational change in IMP dehydrogenase (2011), Biochemistry, 50, 8508-8518.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.205 K+ the K+ dependence of kcat value derives from the rate of flap closure, which increases by more than 65fold in the presence of K+. When K+ is replaced with a dummy ion, the residues of the K+ binding site relax into ordered secondary structure, creating a barrier to conformational exchange. K+ mobilizes these residues by providing alternate interactions for the main chain carbonyls. So K+ changes the shape of the energy well, shrinking the reaction coordinate by shifting the closed conformation toward the open state Cryptosporidium parvum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.205 NAD+
-
 Cryptosporidium parvum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.205 0.14
-
 NAD+ presence of 1 mM K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 0.19
-
 3-acetylpyridine adenine dinucleotide presence of 100 mM K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 0.22
-
 3-acetylpyridine adenine dinucleotide absence of K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 1.4
-
 NAD+ absence of K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 2.4
-
 NAD+ presence of 1 mM K+, pH 8.0, 25°C Cryptosporidium parvum

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.205 Cryptosporidium parvum Q8T6T2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.205 inosine 5'-diphosphate + NAD+ + H2O
-
 Cryptosporidium parvum xanthosine 5'-diphosphate + NADH + H+
-
 ?
1.1.1.205 inosine 5'-phosphate + 3-acetylpyridine adenine dinucleotide + H2O
-
 Cryptosporidium parvum xanthosine 5'-phosphate + reduced 3-acetylpyridine adenine dinucleotide
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.205 0.16
-
 3-acetylpyridine adenine dinucleotide absence of K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 0.27
-
 NAD+ absence of K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 0.8
-
 NAD+ presence of 1 mM K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 2.6
-
 NAD+ presence of 1 mM K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 3
-
 3-acetylpyridine adenine dinucleotide presence of 100 mM K+, pH 8.0, 25°C Cryptosporidium parvum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.205 3-acetylpyridine adenine dinucleotide
-
 Cryptosporidium parvum
1.1.1.205 NAD+
-
 Cryptosporidium parvum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.205 0.6
-
 NAD+ absence of K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 1.5
-
 NAD+ presence of 1 mM K+, pH 8.0, 25°C Cryptosporidium parvum
1.1.1.205 4.9
-
 NAD+ presence of 100 mM K+, pH 8.0, 25°C Cryptosporidium parvum