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

BRENDA support

Literature summary for 7.1.1.1 extracted from

  • Meuller, J.; Zhang, J.; Hou, C.; Bragg, P.D.; Rydstrom, J.
    Properties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase (1997), Biochem. J., 324, 681-687.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.1.1

Protein Variants

Protein Variants Comment Organism
C292T/C339T/C395S/C397T/C435S cysteine of the alpha subunits replaced, similar activity as wild-type Escherichia coli
C292T/C339T/C395S/C397T/C435S/C147S/C260S all 7 cysteines of the enzyme, 5 localized in the alpha subunit and 2 in the beta subunit, are replaced, the cysteine-free mutant shows about 5fold more activity in the reduction of acetylpyridine adenine dinucleotide by NADH than wild-type, the cyclic reduction of acetylpyridine adenine dinucleotide by NADH via NADPH is 2-2.5fold more activ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide cysteine-free mutant enzyme is not inhibited Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0017
-
 NADH wild-type enzyme Escherichia coli
0.002
-
 NADH cysteine-free enzyme Escherichia coli
0.0051
-
 NADPH cysteine-free enzyme Escherichia coli
0.008
-
 thio-NADP+ wild-type enzyme Escherichia coli
0.015
-
 NADPH wild-type enzyme Escherichia coli
0.018
-
 thio-NADP+ cysteine-free enzyme Escherichia coli
0.02
-
 oxidized acetylpyridine adenine dinucleotide cysteine-free enzyme Escherichia coli
0.026
-
 oxidized acetylpyridine adenine dinucleotide wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.2
-
 reduction of NADP+ by NADH driven by electron transport, cysteine-free enzyme reconstituted in membrane vesicles Escherichia coli
0.42
-
 reduction of NADP+ by NADH driven by electron transport, wild-type enzyme reconstituted in membrane vesicles Escherichia coli
1.9
-
 reduction of acetylpyridine adenine dinucleotide by NADPH, cysteine-free enzyme reconstituted in membrane vesicles Escherichia coli
3
-
 reduction of acetylpyridine adenine dinucleotide by NADPH, wild-type enzyme reconstituted in membrane vesicles Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli
NADH
-
 Escherichia coli
NADP+
-
 Escherichia coli
NADPH
-
 Escherichia coli