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

BRENDA support

Literature summary for 1.1.1.205 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
Search for more literature for 1.1.1.205

Activating Compound

Activating Compound Comment Organism Structure
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

Inhibitors Comment Organism Structure
NAD+
-
 Cryptosporidium parvum

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum Q8T6T2
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

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

Ki Value [mM]

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