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Literature summary for 7.1.1.2 extracted from

  • Waletko, A.; Zwicker, K.; Abdrakhmanova, A.; Zickermann, V.; Brandt, U.; Kerscher, S.
    Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity (2005), J. Biol. Chem., 280, 5622-5625.
    View publication on PubMed
Search for more literature for 7.1.1.2

Protein Variants

Protein Variants Comment Organism
H129A fully assembled but destabilized enzyme, without deamino-NADH:ubiquinone oxidoreductase activity Yarrowia lipolytica

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Yarrowia lipolytica 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
4Fe-4S
-
 Yarrowia lipolytica

Organism

Organism UniProt Comment Textmining
Yarrowia lipolytica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-affinity chromatography and gel filtration Yarrowia lipolytica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.62
-
 mutant enzyme H129A, using hexamineruthenium(III)-chloride as substrate Yarrowia lipolytica
0.84
-
 wild type enzyme, using hexamineruthenium(III)-chloride as substrate Yarrowia lipolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + hexamineruthenium(III)-chloride
-
 Yarrowia lipolytica NAD+ + ?
-
 ?
NADH + ubiquinone
-
 Yarrowia lipolytica NAD+ + ubiquinol
-
 ?

Synonyms

Synonyms Comment Organism
complex I
-
 Yarrowia lipolytica
NADH:ubiquinone oxidoreductase
-
 Yarrowia lipolytica

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Yarrowia lipolytica