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Literature summary for 1.6.1.2 extracted from

  • Hickman, J.W.; Barber, R.D.; Skaar, E.P.; Donohue, T.J.
    Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides (2002), J. Bacteriol., 184, 400-409.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.1.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Cereibacter sphaeroides

Protein Variants

Protein Variants Comment Organism
additional information enzyme deficient mutants created by insertions at condon 474, 128, and 285 of ptnA Cereibacter sphaeroides

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Cereibacter sphaeroides 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + NADP+ Cereibacter sphaeroides links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH, provides reducing agent for glutathione and is therefore important for the oxidative stress defense NAD+ + NADPH
-
 r

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
 native and enzyme deficient mutant, mutant strain accumulates higher levels of glutathione disulfide
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 no activity detected with the insertion mutants Cereibacter sphaeroides
50.8
-
 native enzyme with acetylpyridine-NAD+ a n NADPH as substrates, pH 7.0 Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + NADP+
-
 Cereibacter sphaeroides NAD+ + NADPH
-
 r
NADH + NADP+ links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH, provides reducing agent for glutathione and is therefore important for the oxidative stress defense Cereibacter sphaeroides NAD+ + NADPH
-
 r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
-
 Cereibacter sphaeroides NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD(P)+
-
 Cereibacter sphaeroides
NAD(P)H
-
 Cereibacter sphaeroides