Literature summary for 1.14.19.1 extracted from
Yang, Y.S.; Broadwater, J.A.; Pulver, S.C.; Fox, B.G.; Solomon, E.I.
Circular dichroism and magnetic circular dichroism studies of the reduced binuclear non-heme iron site of stearoyl-ACP DELTA9-desaturase: substrate binding and comparison to ribonucleotide reductase (1999), J. Am. Chem. Soc., 121, 2770-2783.
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
coexpression of acyl carrier protein isoform I gene and holo-acyl carrier protein synthase of Escherichia coli |
Spinacia oleracea |
Localization
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
membrane |
bound |
Spinacia oleracea |
16020 |
- |
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Fe2+ |
each subunit of homodimer contains one binuclear non-heme iron active site. The reduced DELTA9-desaturase has two approximately equivalent 5-coordinate irons in a distorted square pyramidal geometry, a two-in-two-out equatorial distortion, the irons are rhombic, weakly antiferromagnetically coupled. Addition of substrate causes dramatic changes, first ion remains 5-coordinate but is distorted toward a trigonal bipyramidal structure, second iron changes to 4-coordinate |
Spinacia oleracea |
|
Molecular Weight [Da]
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
40000 |
- |
homodimer, 2 * 40000 |
Spinacia oleracea |
Natural Substrates/ Products (Substrates)
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
stearoyl-acyl-carrier protein + AH2 + O2 |
Spinacia oleracea |
insertion of a cis double bond between the 9 and 10 position, essential step in fatty acid biosynthesis |
oleoyl-acyl-carrier protein + A + H2O |
- |
? |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Spinacia oleracea |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
- |
Spinacia oleracea |
Reaction
Reaction |
Comment |
Organism |
Reaction ID |
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
the possible mechanism would be that dioxygen has to bind to both irons for effective two-electron transfer to the half-occupied antibonding pi orbitals of dioxygen to give a peroxide level intermediate |
Spinacia oleracea |
|
Storage Stability
Storage Stability |
Organism |
reduced enzyme is stable under O2 for hours |
Spinacia oleracea |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
stearoyl-acyl-carrier protein + AH2 + O2 |
insertion of a cis double bond between the 9 and 10 position, essential step in fatty acid biosynthesis |
Spinacia oleracea |
oleoyl-acyl-carrier protein + A + H2O |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
dimer |
homodimer, 2 * 40000 |
Spinacia oleracea |
Turnover Number [1/s]
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
0.5 |
- |
stearoyl-acyl-carrier protein |
- |
Spinacia oleracea |
|
Cofactor
Cofactor |
Comment |
Organism |
Structure |
NADPH |
- |
Spinacia oleracea |
|