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Literature summary for 1.1.1.205 extracted from

  • Josephine, H.R.; Ravichandran, K.R.; Hedstrom, L.
    The Cys319 loop modulates the transition between dehydrogenase and hydrolase conformations in inosine 5-monophosphate dehydrogenase (2010), Biochemistry, 49, 10674-10681.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.205

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structures. The Cys319 loop has different conformations during the dehydrogenase and hydrolase reactions as suggested by the crystal structures. The structure of the Cys319 loop modulates the closure of themobile flap. This conformational change converts the enzyme from a dehydrogenase into hydrolase, suggesting that the conformation of the Cys319 loop may gate the catalytic cycle Tritrichomonas suis

Protein Variants

Protein Variants Comment Organism
E323A substitution increases the equilibrium constant for the dehydrogenase step but decreases the equilibrium between open and closed conformations of a mobile flap Tritrichomonas suis
Q324A substitution increases the equilibrium constant for the dehydrogenase step but decreases the equilibrium between open and closed conformations of a mobile flap Tritrichomonas suis
R322A substitution increases the equilibrium constant for the dehydrogenase step but decreases the equilibrium between open and closed conformations of a mobile flap Tritrichomonas suis
R322E substitution decreases the rates of hydride transfer and hydrolysis by factors of 2000 and 130, respectively Tritrichomonas suis

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Tritrichomonas suis
tiazofurin
-
 Tritrichomonas suis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information analysis of microscopic rate constants Tritrichomonas suis
0.12
-
 NAD+ mutant Q324A, pH 8.0, 25°C Tritrichomonas suis
0.15
-
 NAD+ wild-type, pH 8.0, 25°C Tritrichomonas suis
0.3
-
 NAD+ mutant E323A, pH 8.0, 25°C Tritrichomonas suis
0.91
-
 NAD+ mutant R322A, pH 8.0, 25°C Tritrichomonas suis
1.7
-
 inosine 5'-phosphate wild-type, pH 8.0, 25°C Tritrichomonas suis
2.6
-
 NAD+ mutant R322E, pH 8.0, 25°C Tritrichomonas suis
7.6
-
 inosine 5'-phosphate mutant R322A, pH 8.0, 25°C Tritrichomonas suis
28
-
 inosine 5'-phosphate mutant Q324A, pH 8.0, 25°C Tritrichomonas suis
31
-
 inosine 5'-phosphate mutant E323A, pH 8.0, 25°C Tritrichomonas suis

Organism

Organism UniProt Comment Textmining
Tritrichomonas suis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
inosine 5'-phosphate + NAD+
-
 Tritrichomonas suis xanthosine 5'-phosphate + NADH + H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.009
-
 inosine 5'-phosphate mutant R322E, pH 8.0, 25°C Tritrichomonas suis
0.36
-
 inosine 5'-phosphate mutant R322A, pH 8.0, 25°C Tritrichomonas suis
0.43
-
 inosine 5'-phosphate mutant Q324A, pH 8.0, 25°C Tritrichomonas suis
1.1
-
 inosine 5'-phosphate mutant E323A, pH 8.0, 25°C Tritrichomonas suis
1.9
-
 inosine 5'-phosphate wild-type, pH 8.0, 25°C Tritrichomonas suis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2 5 ADP mutant E323A, pH 8.0, 25°C Tritrichomonas suis
7
-
 ADP mutant Q324A, pH 8.0, 25°C Tritrichomonas suis
17
-
 ADP mutant R322A, pH 8.0, 25°C Tritrichomonas suis
31
-
 ADP wild-type, pH 8.0, 25°C Tritrichomonas suis
50
-
 ADP mutant R322E, pH 8.0, 25°C Tritrichomonas suis
69
-
 tiazofurin wild-type, pH 8.0, 25°C Tritrichomonas suis
90
-
 tiazofurin mutant Q324A, pH 8.0, 25°C Tritrichomonas suis
91
-
 tiazofurin mutant R322A, pH 8.0, 25°C Tritrichomonas suis
200
-
 tiazofurin mutant R322E, pH 8.0, 25°C Tritrichomonas suis
300
-
 tiazofurin mutant E323A, pH 8.0, 25°C Tritrichomonas suis