Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bewley, M.C.; Davis, C.A.; Marohnic, C.C.; Taormina, D.; Barber, M.J.
    The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site (2003), Biochemistry, 42, 13145-13151.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 wild type and mutant enzyme expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.2.2 sitting drop method Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 S127P caused methemoglobinemia type II, FAD is displaced from its binding site by NADH, Km for NADH is strongly increased Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.2 0.003
-
 NADH pH 7.0, wild type enzyme with cytochrome b5 as substrate Rattus norvegicus
1.6.2.2 0.006
-
 NADH pH 7.0, wild type enzyme with ferricyanide as substrate Rattus norvegicus
1.6.2.2 0.007
-
 ferricyanide pH 7.0, wild type enzyme Rattus norvegicus
1.6.2.2 0.008
-
 ferricyanide pH 7.0, S127P mutant enzyme Rattus norvegicus
1.6.2.2 0.013
-
 ferricytochrome b5 pH 7.0, wild type enzyme Rattus norvegicus
1.6.2.2 0.014
-
 ferricytochrome b5 pH 7.0, S127P mutant enzyme Rattus norvegicus
1.6.2.2 0.025
-
 NADH pH 7.0, S127P mutant enzyme with cytochrome b5 as substrate Rattus norvegicus
1.6.2.2 0.055
-
 NADH pH 7.0, S127P mutant enzyme with ferricyanide as substrate Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 membrane full length form contains a 3 kDa membrane anchoring domain Rattus norvegicus 16020
-
1.6.2.2 microsome
-
 Rattus norvegicus
-
-
1.6.2.2 soluble truncated form lacking the membrane anchoring domain Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH Rattus norvegicus involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 recombinant enzymes purified from Escherichia coli Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Rattus norvegicus 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II Rattus norvegicus 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.2 106
-
 ferricytochrome b5 pH 7.0, S127P mutant enzyme Rattus norvegicus
1.6.2.2 300
-
 ferricyanide pH 7.0, S127P mutant enzyme Rattus norvegicus
1.6.2.2 367
-
 ferricytochrome b5 pH 7.0, wild type enzyme Rattus norvegicus
1.6.2.2 800
-
 ferricyanide pH 7.0, wild type enzyme Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 FAD tightly bound prosthetic group Rattus norvegicus
1.6.2.2 NADH
-
 Rattus norvegicus