Literature summary for 1.6.1.1 extracted from

Voordouw, G.; van der Vies, S.M.; Eweg, J.K.; Veeger, C.; van Breemen, J.F.L.; van Bruggen, E.F.J.
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers (1980), Eur. J. Biochem., 111, 347-355.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Azotobacter vinelandii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
52000	-	x * 52000, SDS-PAGE, immunoblot	Azotobacter vinelandii
54000	-	8 * 54000, four subunits are placed in a rhomb, a second tetramer is located staggered on top of the first one, deduced from amino acid analysis and electron micrography of purified enzyme	Azotobacter vinelandii

Organism

Organism	UniProt	Comment	Textmining
Azotobacter vinelandii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
affinity chromatography	Azotobacter vinelandii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
575	-	-	Azotobacter vinelandii

Subunits

Subunits	Comment	Organism
octamer	x * 52000, SDS-PAGE, immunoblot	Azotobacter vinelandii
octamer	8 * 54000, four subunits are placed in a rhomb, a second tetramer is located staggered on top of the first one, deduced from amino acid analysis and electron micrography of purified enzyme	Azotobacter vinelandii

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Release 2023.1 (January 2023)