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

BRENDA support

Literature summary for 1.6.1.2 extracted from

  • Singh, A.; Venning, J.D.; Quirk, P.G.; van Boxel, G.I.; Rodrigues, D.J.; White, S.A.; Jackson, J.B.
    Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation (2003), J. Biol. Chem., 278, 33208-33216.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information electrochemical gradient forces reaction Rhodospirillum rubrum
additional information electrochemical gradient forces reaction Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
dI and native and E155W mutant of dIII expressed in Escherichia coli Rhodospirillum rubrum
dIII domain expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
dI2dIII complex in its thio-NAD+/NADP+ form Rhodospirillum rubrum
dIII domain in its thio-NADP+ form Homo sapiens

Protein Variants

Protein Variants Comment Organism
E155W dIII domain, displays similar catalytic properties as wild type, introduced tryptophan fluorescence is sensitive to the redox state of the bound nucleotide Rhodospirillum rubrum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Rhodospirillum rubrum 16020
-
mitochondrial membrane
-
Homo sapiens 31966
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + NADP+ Rhodospirillum rubrum links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane NAD+ + NADPH
-
r
NADH + NADP+ Homo sapiens links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane NAD+ + NADPH
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13423
-
-
Rhodospirillum rubrum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + NADP+
-
Rhodospirillum rubrum NAD+ + NADPH
-
r
NADH + NADP+
-
Homo sapiens NAD+ + NADPH
-
r
NADH + NADP+ links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane Rhodospirillum rubrum NAD+ + NADPH
-
r
NADH + NADP+ links hydride transfer between NAD(H) and NADP(H) to the outside-in translocation of protons across membrane Homo sapiens NAD+ + NADPH
-
r
NADH + oxidized 3-acetylpyridine adenine dinucleotide
-
Rhodospirillum rubrum NAD+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
NADH + thio-NADP+ good substrate Rhodospirillum rubrum NAD+ + thio-NADPH
-
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
-
Rhodospirillum rubrum NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
thio-NADH + NADP+ poor substrate Rhodospirillum rubrum thio-NAD+ + NADPH
-
r

Subunits

Subunits Comment Organism
dimer two monomers with dI, dII, and dIII domain structure Rhodospirillum rubrum
dimer two monomers with dI, dII, and dIII domain structure Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD(P)+
-
Rhodospirillum rubrum
NAD(P)+
-
Homo sapiens
NAD(P)H
-
Rhodospirillum rubrum
NAD(P)H
-
Homo sapiens