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

BRENDA support

Literature summary for 1.6.1.1 extracted from

  • Chung, A.E.
    Pyridine nucleotide transhydrogenase from Azotobacter vinelandii (1970), J. Bacteriol., 102, 438-447.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.1.1

Activating Compound

Activating Compound Comment Organism Structure
2'-AMP activation of reduction of NADP+ or thio-NAD+ by NADH, no effect on reduction of NAD+ or thio-NAD+ by NADPH Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
NAD+ competitive to thio-NAD+, uncompetitive with respect to NADPH Azotobacter vinelandii
NADP+ uncompetitive to thio-NAD+ Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 thio-NAD+ cosubstrate NADH Azotobacter vinelandii
0.077
-
 NADH + thio-NAD+ Azotobacter vinelandii
0.25
-
 thio-NAD+ cosubstrate NADPH Azotobacter vinelandii
0.38
-
 NAD+ cosubstrate NADPH Azotobacter vinelandii
0.4
-
 deamino-NAD+ cosubstrate NADPH Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
251
-
-
 Azotobacter vinelandii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADP+ + NADH
-
 Azotobacter vinelandii NADPH + NAD+
-
 ?
NADPH + deamino-NAD+
-
 Azotobacter vinelandii NADP+ + deamino-NADH
-
 ?
NADPH + thio-NADP+ + H+[side 1]
-
 Azotobacter vinelandii NADP+ + thio-NADPH + H+[side 2]
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 35
-
 Azotobacter vinelandii