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Literature summary for 1.14.19.1 extracted from

  • Strittmatter, P.; Enoch, H.G.
    Purification of stearyl-CoA desaturase from liver (1978), Methods Enzymol., 52, 188-193.
    View publication on PubMed

General Stability

General Stability Organism
relatively labil Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
CN- at high concentrations Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information substrates with 14-19 carbon fatty acyl chains show similar Km values of 0.0045-0.005 mM Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rattus norvegicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ contains one atom of non-heme iron per enzyme molecule, catalytic function Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
stearoyl-CoA + AH2 + O2 Rattus norvegicus
-
oleoyl-CoA + A + H2O
-
?
stearoyl-CoA + AH2 + O2 Rattus norvegicus Long-Evans
-
oleoyl-CoA + A + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
Long-Evans
-
Rattus norvegicus Long-Evans
-
Long-Evans
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information no detectable carbohydrate Rattus norvegicus
phospholipoprotein 4-12 mol of phospholipid per mol of polypeptide Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
different fractions by sonication and centrifugation, ion-exchange Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.325
-
-
Rattus norvegicus

Storage Stability

Storage Stability Organism
-75°C, more than 95% pure last fraction, 3 months, no loss of activity Rattus norvegicus
-75°C, fractions during purification, overnight, 20-50% loss of activity Rattus norvegicus
0°C, above 95% pure last fraction, 15-20 hours, 30-50% loss of activity Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 12-19 carbon fatty acyl chains undergo 9,10 desaturation. Dephospho-, deamino- and (1-N6-etheno)-CoA analogs of stearoyl-CoA are poorer substrates than stearoyl-CoA Rattus norvegicus ?
-
?
additional information 12-19 carbon fatty acyl chains undergo 9,10 desaturation. Dephospho-, deamino- and (1-N6-etheno)-CoA analogs of stearoyl-CoA are poorer substrates than stearoyl-CoA Rattus norvegicus Long-Evans ?
-
?
stearoyl-CoA + AH2 + O2
-
Rattus norvegicus oleoyl-CoA + A + H2O
-
?
stearoyl-CoA + AH2 + O2
-
Rattus norvegicus Long-Evans oleoyl-CoA + A + H2O
-
?
stearoyl-CoA + NADH + O2
-
Rattus norvegicus oleoyl-CoA + NAD+ + H2O
-
?
stearoyl-CoA + NADH + O2
-
Rattus norvegicus Long-Evans oleoyl-CoA + NAD+ + H2O
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.35
-
stearoyl-CoA fatty acyl-CoA substrates with chain length of 14-19 carbon atoms show similar turnover number of about 22 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Rattus norvegicus