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

BRENDA support

Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.1 C292T/C339T/C395S/C397T/C435S cysteine of the alpha subunits replaced, similar activity as wild-type Escherichia coli
7.1.1.1 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.1 0.0017
-
NADH wild-type enzyme Escherichia coli
7.1.1.1 0.002
-
NADH cysteine-free enzyme Escherichia coli
7.1.1.1 0.0051
-
NADPH cysteine-free enzyme Escherichia coli
7.1.1.1 0.008
-
thio-NADP+ wild-type enzyme Escherichia coli
7.1.1.1 0.015
-
NADPH wild-type enzyme Escherichia coli
7.1.1.1 0.018
-
thio-NADP+ cysteine-free enzyme Escherichia coli
7.1.1.1 0.02
-
oxidized acetylpyridine adenine dinucleotide cysteine-free enzyme Escherichia coli
7.1.1.1 0.026
-
oxidized acetylpyridine adenine dinucleotide wild-type enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.1 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.1.1.1 0.2
-
reduction of NADP+ by NADH driven by electron transport, cysteine-free enzyme reconstituted in membrane vesicles Escherichia coli
7.1.1.1 0.42
-
reduction of NADP+ by NADH driven by electron transport, wild-type enzyme reconstituted in membrane vesicles Escherichia coli
7.1.1.1 1.9
-
reduction of acetylpyridine adenine dinucleotide by NADPH, cysteine-free enzyme reconstituted in membrane vesicles Escherichia coli
7.1.1.1 3
-
reduction of acetylpyridine adenine dinucleotide by NADPH, wild-type enzyme reconstituted in membrane vesicles Escherichia coli

Cofactor

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