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

BRENDA support

Literature summary for 1.6.2.2 extracted from

  • Maeda, S.; Kobori, H.; Tanigawa, M.; Sato, K.; Yubisui, T.; Hori, H.; Nagata, Y.
    Methemoglobin reduction by NADH-cytochrome b(5) reductase in Propsilocerus akamusi larvae (2015), Comp. Biochem. Physiol. B, 185, 54-61 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
benzoate complete inhibition at 1 mM Propsilocerus akamusi
Ca2+ 23.5% residual activity at 1 mM Propsilocerus akamusi
dithiothreitol 80% residual activity at 1 mM Propsilocerus akamusi
iodoacetamide 23.5% residual activity at 1 mM Propsilocerus akamusi
iodoacetate 27.3% residual activity at 1 mM Propsilocerus akamusi
additional information the enzyme is not inhibited by Mg2+, Mn2+, or EDTA Propsilocerus akamusi
NaCN 91.4% residual activity at 1 mM Propsilocerus akamusi
p-hydroxymercuribenzoate complete inhibition at 1 mM Propsilocerus akamusi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.328
-
oxidized 2,6-dichlorophenolindophenol at pH 6.4 and 25°C Propsilocerus akamusi
0.345
-
ferricyanide at pH 6.4 and 25°C Propsilocerus akamusi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33200
-
gel filtration Propsilocerus akamusi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + ferricytochrome b5 Propsilocerus akamusi
-
NAD+ + H+ + ferrocytochrome b5
-
?

Organism

Organism UniProt Comment Textmining
Propsilocerus akamusi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-cellulose column chromatography, Toyopearl butyl column chromatography, and Sephacryl S200 gel filtration Propsilocerus akamusi

Source Tissue

Source Tissue Comment Organism Textmining
larva
-
Propsilocerus akamusi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + ferricyanide
-
Propsilocerus akamusi NAD+ + H+ + ferrocyanide
-
?
NADH + ferricytochrome b5
-
Propsilocerus akamusi NAD+ + H+ + ferrocytochrome b5
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
-
Propsilocerus akamusi NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
?

Subunits

Subunits Comment Organism
monomer 1 * 37000, SDS-PAGE Propsilocerus akamusi

Synonyms

Synonyms Comment Organism
NADH-b5R
-
Propsilocerus akamusi
NADH-cytochrome b5 reductase
-
Propsilocerus akamusi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
Propsilocerus akamusi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4
-
the enzyme shows two peaks of activity at pH 6.4 and 8.2 Propsilocerus akamusi
8.2
-
the enzyme shows two peaks of activity at pH 6.4 and 8.2 Propsilocerus akamusi

Cofactor

Cofactor Comment Organism Structure
FAD
-
Propsilocerus akamusi