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Literature summary for 1.6.2.2 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
Search for more literature for 1.6.2.2

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
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]

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome b5 + NADH
-
 Rattus norvegicus 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
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]

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

Cofactor

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