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Literature summary extracted from

  • Kervinen, M.; Hinttala, R.; Helander, H.M.; Kurki, S.; Uusimaa, J.; Finel, M.; Majamaa, K.; Hassinen, I.E.
    The MELAS mutations 3946 and 3949 perturb the critical structure in a conserved loop of the ND1 subunit of mitochondrial complex I (2006), Hum. Mol. Genet., 15, 2543-2552.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.2 D213E reduced activity Escherichia coli
7.1.1.2 D213N reduced activity Escherichia coli
7.1.1.2 E214K inactive mutant Escherichia coli
7.1.1.2 E216A reduced activity Escherichia coli
7.1.1.2 E228D reduced activity Escherichia coli
7.1.1.2 E228K reduced activity Escherichia coli
7.1.1.2 E228Q reduced activity Escherichia coli
7.1.1.2 E234D mutant with slightly reduced activity compared to the wild type enzyme Paracoccus denitrificans
7.1.1.2 E234Q mutant with strongly reduced activity compared to the wild type enzyme Paracoccus denitrificans
7.1.1.2 H210F reduced activity Escherichia coli
7.1.1.2 H210T reduced activity Escherichia coli
7.1.1.2 R209F reduced activity Escherichia coli
7.1.1.2 R209H reduced activity Escherichia coli
7.1.1.2 R209K reduced activity Escherichia coli
7.1.1.2 V206E reduced activity Escherichia coli
7.1.1.2 Y229H 30% lower activity than wild type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.2 vanillylnonanamide 0.4 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.2 2 3 decylubiquinone mutant enzyme V206E Escherichia coli
7.1.1.2 2 3 decylubiquinone mutant enzyme Y229H Escherichia coli
7.1.1.2 25
-
 decylubiquinone mutant enzyme H210T Escherichia coli
7.1.1.2 33
-
 decylubiquinone mutant enzyme D213E Escherichia coli
7.1.1.2 34
-
 decylubiquinone mutant enzyme D213N Escherichia coli
7.1.1.2 37
-
 decylubiquinone mutant enzyme R209F Escherichia coli
7.1.1.2 40
-
 decylubiquinone mutant enzyme E228D Escherichia coli
7.1.1.2 43
-
 decylubiquinone wild type enzyme Escherichia coli
7.1.1.2 43
-
 decylubiquinone mutant enzyme E216A Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 mitochondrion
-
 Escherichia coli 5739
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.2 Escherichia coli
-
-
-
7.1.1.2 Escherichia coli GV102
-
-
-
7.1.1.2 Paracoccus denitrificans
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.1.1.2 0.0098
-
 mutant enzyme E234Q, using ubiquinone-1 as substrate Paracoccus denitrificans
7.1.1.2 0.15
-
 mutant enzyme E234Q, using hexammineruthenium-(III)-chloride as substrate Paracoccus denitrificans
7.1.1.2 0.161
-
 wild type enzyme, using ubiquinone-1 as substrate Paracoccus denitrificans
7.1.1.2 0.163
-
 mutant enzyme E228Q, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.175
-
 mutant enzyme E234D, using ubiquinone-1 as substrate Paracoccus denitrificans
7.1.1.2 0.211
-
 mutant enzyme R209H, using NADH as substrate Escherichia coli
7.1.1.2 0.213
-
 mutant enzyme E228K, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.229
-
 mutant enzyme R209F, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.245
-
 mutant enzyme D213E, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.249
-
 mutant enzyme R209H, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.256
-
 mutant enzyme R209F, using NADH as substrate Escherichia coli
7.1.1.2 0.259
-
 mutant enzyme V206E, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.265
-
 mutant enzyme R209K, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.268
-
 mutant enzyme H210T, using NADH as substrate Escherichia coli
7.1.1.2 0.268
-
 mutant enzyme R209K, using NADH as substrate Escherichia coli
7.1.1.2 0.274
-
 mutant enzyme E228K, using NADH as substrate Escherichia coli
7.1.1.2 0.274
-
 mutant enzyme Y229H, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.305
-
 mutant enzyme E228D, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.31
-
 mutant enzyme H210F, using NADH as substrate Escherichia coli
7.1.1.2 0.313
-
 mutant enzyme V206E, using NADH as substrate Escherichia coli
7.1.1.2 0.316
-
 mutant enzyme H210T, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.32
-
 mutant enzyme E228Q, using NADH as substrate Escherichia coli
7.1.1.2 0.324
-
 mutant enzyme D213E, using NADH as substrate Escherichia coli
7.1.1.2 0.329
-
 mutant enzyme H210F, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.341
-
 mutant enzyme D213N, using NADH as substrate Escherichia coli
7.1.1.2 0.348
-
 mutant enzyme Y229H, using NADH as substrate Escherichia coli
7.1.1.2 0.354
-
 mutant enzyme E216A, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.368
-
 mutant enzyme D213N, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 0.424
-
 mutant enzyme E228D, using NADH as substrate Escherichia coli
7.1.1.2 0.442
-
 mutant enzyme E216A, using NADH as substrate Escherichia coli
7.1.1.2 0.63
-
 wild type enzyme, using NADH as substrate Escherichia coli
7.1.1.2 0.8
-
 wild type enzyme, using hexammineruthenium-(III)-chloride as substrate Escherichia coli
7.1.1.2 1.144
-
 wild type enzyme, using hexammineruthenium-(III)-chloride as substrate Paracoccus denitrificans
7.1.1.2 1.34
-
 mutant enzyme E234D, using hexammineruthenium-(III)-chloride as substrate Paracoccus denitrificans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + decylubiquinone
-
 Paracoccus denitrificans NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + decylubiquinone
-
 Escherichia coli NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + decylubiquinone
-
 Escherichia coli GV102 NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + hexammineruthenium-(III)-chloride
-
 Paracoccus denitrificans NAD+ + ?
-
 ?
7.1.1.2 NADH + hexammineruthenium-(III)-chloride
-
 Escherichia coli NAD+ + ?
-
 ?
7.1.1.2 NADH + hexammineruthenium-(III)-chloride
-
 Escherichia coli GV102 NAD+ + ?
-
 ?
7.1.1.2 NADH + ubiquinone
-
 Escherichia coli NAD+ + ubiquinol
-
 ?
7.1.1.2 NADH + ubiquinone
-
 Escherichia coli GV102 NAD+ + ubiquinol
-
 ?
7.1.1.2 NADH + ubiquinone-1
-
 Paracoccus denitrificans NAD+ + ubiquinol-1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.1.1.2 complex I in mitochondria Paracoccus denitrificans
7.1.1.2 complex I in mitochondria Escherichia coli
7.1.1.2 ND1
-
 Paracoccus denitrificans
7.1.1.2 ND1
-
 Escherichia coli
7.1.1.2 NDH-1 in bacteria Paracoccus denitrificans
7.1.1.2 NDH-1 in bacteria Escherichia coli
7.1.1.2 proton-pumping NADH-ubiquinone oxidoreductase
-
 Paracoccus denitrificans
7.1.1.2 proton-pumping NADH-ubiquinone oxidoreductase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 NADH
-
 Paracoccus denitrificans
7.1.1.2 NADH
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
7.1.1.2 30
-
 vanillylnonanamide mutant enzyme D213E Escherichia coli
7.1.1.2 40
-
 vanillylnonanamide wild type enzyme Escherichia coli
7.1.1.2 41
-
 vanillylnonanamide mutant enzyme D213N Escherichia coli
7.1.1.2 43
-
 vanillylnonanamide mutant enzyme E228D Escherichia coli