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Literature summary extracted from

  • Yamaguchi, M.; Hatefi, Y.
    Energy-transducing nicotinamide nucleotide transhydrogenase. Nucleotide binding properties of the purified enzyme and proteolytic fragments (1993), J. Biol. Chem., 268, 17871-17877.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.1.2 N,N'-Dicylclohexylcarbodiimide
-
 Bos taurus
1.6.1.2 N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline 1.8 mM, complete inactivation after 55 min, approx. 25% inactivation after 55 min in the presence of 4 mM NMNH Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.1.2 109065
-
 2 * 109065, monomer is composed of three domains: a 430 residue long N-terminal hydrophilic domain called dI, a 400 residue long central hydrophobic domain that intercalates into the membrane called dII, and a 200 residue long C-terminal hydrophilic domain called dIII Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.6.1.2 Bos taurus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.6.1.2 NADPH + NAD+ = NADP+ + NADH mitochondrial proton-motive force accelerates the rate of NADPH formation 10-12fold and shifts the equilibrium in the direction of product formation Bos taurus
a

Subunits

EC Number Subunits Comment Organism
1.6.1.2 dimer 2 * 109065, monomer is composed of three domains: a 430 residue long N-terminal hydrophilic domain called dI, a 400 residue long central hydrophobic domain that intercalates into the membrane called dII, and a 200 residue long C-terminal hydrophilic domain called dIII Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.1.2 NAD+
-
 Bos taurus
1.6.1.2 NADH
-
 Bos taurus
1.6.1.2 NADP+
-
 Bos taurus
1.6.1.2 NADPH
-
 Bos taurus