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Literature summary extracted from

  • Bewley, M.C.; Marohnic, C.C.; Barber, M.J.
    The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent (2001), Biochemistry, 40, 13574-13582.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 expression of wild-type, K110R, K110H, K110A, K110E and K110Q mutant enzymes in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.2.2 sitting drop method, reservoir: 8% poly ethylene glycol 6000, 5% 2-methyl-2,4-pentanediol in 100 mM 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid, pH 7.5, X-ray structure, resolution: enzyme 2.0 A, enzyme-NAD+ complex, 2.3 A Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 K110A strongly reduced kcat for ferricyanide and cytochrome b5 Rattus norvegicus
1.6.2.2 K110E strongly reduced kcat for ferricyanide and cytochrome b5 Rattus norvegicus
1.6.2.2 K110H strongly reduced kcat for ferricyanide and cytochrome b5 Rattus norvegicus
1.6.2.2 K110Q very low kcat for ferricyanide and cytochrome b5 Rattus norvegicus
1.6.2.2 K110R reduced kcat for ferricyanid and cytochrome b5 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.2 0.003
-
 cytochrome b5 K110Q mutant enzyme Rattus norvegicus
1.6.2.2 0.004
-
 cytochrome b5 K110E mutant enzyme Rattus norvegicus
1.6.2.2 0.005
-
 ferricyanide K110R mutant enzyme Rattus norvegicus
1.6.2.2 0.006
-
 ferricyanide recombinant wild-type enzyme Rattus norvegicus
1.6.2.2 0.009
-
 cytochrome b5 K110R mutant enzyme Rattus norvegicus
1.6.2.2 0.009
-
 cytochrome b5 K110A mutant enzyme Rattus norvegicus
1.6.2.2 0.01
-
 cytochrome b5 recombinant wild-type enzyme Rattus norvegicus
1.6.2.2 0.012
-
 cytochrome b5 K110H mutant enzyme Rattus norvegicus
1.6.2.2 0.05
-
 ferricyanide K110H mutant enzyme Rattus norvegicus
1.6.2.2 0.37
-
 ferricyanide K110E mutant enzyme Rattus norvegicus
1.6.2.2 0.38
-
 ferricyanide K110A mutant enzyme Rattus norvegicus
1.6.2.2 0.76
-
 ferricyanide K110Q mutant enzyme Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Rattus norvegicus P20070
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 wild-type, K110R, K110H, K110A, K110E and K110Q mutant enzymes Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 NADH + ferricytochrome b5
-
 Rattus norvegicus NAD+ + H+ + ferrocytochrome b5
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.2 1
-
 ferricytochrome b5 K110E mutant enzyme Rattus norvegicus
1.6.2.2 4
-
 ferricytochrome b5 K110Q mutant enzyme Rattus norvegicus
1.6.2.2 40
-
 ferricyanide K110Q mutant enzyme Rattus norvegicus
1.6.2.2 90
-
 ferricytochrome b5 K110A mutant enzyme Rattus norvegicus
1.6.2.2 110
-
 ferricytochrome b5 K110H mutant enzyme Rattus norvegicus
1.6.2.2 120
-
 ferricyanide K110E mutant enzyme Rattus norvegicus
1.6.2.2 200
-
 ferricytochrome b5 K110R mutant enzyme Rattus norvegicus
1.6.2.2 270
-
 ferricytochrome b5 recombinant wild-type enzyme Rattus norvegicus
1.6.2.2 270
-
 ferricyanide K110A mutant enzyme Rattus norvegicus
1.6.2.2 340
-
 ferricyanide K110H mutant enzyme Rattus norvegicus
1.6.2.2 470
-
 ferricyanide K110R mutant enzyme Rattus norvegicus
1.6.2.2 800
-
 ferricyanide recombinant wild-type enzyme Rattus norvegicus