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Information on EC 1.14.19.2 - stearoyl-[acyl-carrier-protein] 9-desaturase and Organism(s) Ricinus communis and UniProt Accession P22337

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IUBMB Comments
The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein. The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid. It also acts on palmitoyl-[acyl-carrier-protein] [4,5].
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Ricinus communis
UNIPROT: P22337
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The taxonomic range for the selected organisms is: Ricinus communis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
stearoyl-[acyl-carrier protein]
+
2
reduced ferredoxin [iron-sulfur] cluster
+
O2
+
2
H+
=
oleoyl-[acyl-carrier protein]
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
2
H2O
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
2
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
2
Synonyms
stearoyl-acp desaturase, stearoyl-acyl carrier protein desaturase, sacpd-c, desa1, desa2, zmsad1, sacpd, stearoyl-acyl carrier protein (acp) desaturase, nbsacpd-c, gmsacpd-c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
desaturase, acyl-[acyl carrier protein]
-
-
-
-
stearoyl-ACP desaturase
-
-
-
-
stearoyl-[acyl carrier protein] desaturase
-
-
-
-
stearyl acyl carrier protein desaturase
-
-
-
-
stearyl-ACP desaturase
-
-
-
-
stearyl-acyl carrier protein desaturase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
peroxodiferric intermediate is suggested
stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
EPR and ENDOR studies, both major conformers of the diferric cluster have a mu-oxo bridge, structural alterations upon binding of substrate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
stearoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating)
The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein. The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid. It also acts on palmitoyl-[acyl-carrier-protein] [4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
37256-86-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-(heptyloxy)-decanoyl-[acyl-carrier protein] + reduced acceptor + O2
9-hydroxynonanoyl-[acyl-carrier protein] + n-octanal + acceptor + H2O
show the reaction diagram
-
-
?
7-(decyloxy)-heptanoyl-[acyl-carrier protein] + reduced acceptor + O2
7-dec-1-enyloxyheptanoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
-
-
?
8-(nonyloxy)-octanoyl-[acyl-carrier protein] + reduced acceptor + O2
8-hydroxyoctanoyl-[acyl-carrier protein] + 1-nonanal + acceptor + H2O
show the reaction diagram
-
-
?
9-(octyloxy)-nonanoyl-[acyl-carrier protein] + reduced acceptor + O2
9-hydroxynonanoyl-[acyl-carrier protein] + 1-octanal + acceptor + H2O
show the reaction diagram
-
-
?
heptadecanoyl-[acyl-carrier protein] + reduced ferredoxin + O2
9-heptadecenoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
very low activity, vegetative ferredoxin from Anabaena
-
?
hexadecanoyl-[acyl-carrier protein] + reduced ferredoxin + O2 + H+
9-hexadecenoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
r
nonadecanoyl-[acyl-carrier protein] + reduced ferredoxin + O2
9-nonadecenoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
low activity, vegetative ferredoxin from Anabaena
-
?
octadecanoyl-[acyl-carrier protein] + reduced ferredoxin + O2 + H+
9-octadecenoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
r
pentadecanoyl-[acyl-carrier protein] + reduced ferredoxin + O2
9-pentadecenoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
very low activity, vegetative ferredoxin from Anabaena
-
?
stearoyl-[acyl-carrier protein] + reduced ferredoxin + O2 + H+
oleoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
r
tetradecanoyl-[acyl-carrier protein] + reduced acceptor + O2
9-tetradecenoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
di-iron center
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0074
10-(heptyloxy)-decanoyl-[acyl-carrier protein]
-
0.0066
7-(decyloxy)-heptanoyl-[acyl-carrier protein]
-
0.0059
heptadecanoyl-[acyl-carrier protein]
-
0.00055 - 0.0083
hexadecanoyl-[acyl-carrier protein]
0.0013
nonadecanoyl-[acyl-carrier protein]
-
0.00046 - 0.0039
octadecanoyl-[acyl-carrier protein]
0.069
pentadecanoyl-[acyl-carrier protein]
-
0.001 - 0.0058
tetradecanoyl-[acyl-carrier protein]
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
10-(heptyloxy)-decanoyl-[acyl-carrier protein]
-
0.2
7-(decyloxy)-heptanoyl-[acyl-carrier protein]
-
0.04
8-(nonyloxy)-octanoyl-[acyl-carrier protein]
-
0.02
9-(octyloxy)-nonanoyl-[acyl-carrier protein]
-
0.233
heptadecanoyl-[acyl-carrier protein]
-
0.0467 - 0.422
hexadecanoyl-[acyl-carrier protein]
0.2
nonadecanoyl-[acyl-carrier protein]
-
0.0817 - 0.817
octadecanoyl-[acyl-carrier protein]
0.0317
pentadecanoyl-[acyl-carrier protein]
-
0.333 - 0.5
stearoyl-[acyl-carrier protein]
-
0.0065 - 0.817
tetradecanoyl-[acyl-carrier protein]
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
STAD_RICCO
396
0
45371
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
alpha2, 2 * 37000, recombinant enzyme lacking a putative transit peptide, SDS-PAGE
75000
recombinant enzyme lacking a putative transit peptide
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
alpha2, 2 * 37000, recombinant enzyme lacking a putative transit peptide, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion, 12-18 mg/ml enzyme solution, reservoir solution contains 100 mM cacodylate buffer, pH 5.4, 200 mM magnesium acetate and 12-18% polyethyleneglycol 8000, needle shaped crystals too thin for X-ray study
in complex with azide or acetae, apo- and single-iron form
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L118F/P179I
15fold higher activity with palmitoyl-[acyl-carrier protein] than wild-type enzyme, low DELTA10 desaturase activity
L118W
100% activity with palmitoyl-[acyl-carrier protein], 89% activity with stearoyl-[acyl-carrier protein] and 8.2% activity with myristoyl-[acyl-carrier protein], wild-type is only active with stearoyl-[acyl-carrier protein]
T117R/G188L
82fold higher specificity for palmitoyl-[acyl-carrier protein] with respect to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme lacking a putative transit peptide
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knutzon, D.S.; Scherer, D.E.; Schreckengost, W.E.
Nucleotide sequence of a complementary DNA clone encoding stearoyl-acyl carrier protein desaturase from castor bean, Ricinus communis
Plant Physiol.
96
344-345
1991
Ricinus communis (P22337), Ricinus communis
Manually annotated by BRENDA team
Shanklin, J.; Somerville, C.
Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs
Proc. Natl. Acad. Sci. USA
88
2510-2514
1991
Persea americana, Cucumis sativus, Ricinus communis (P22337), Ricinus communis
Manually annotated by BRENDA team
Schneider, G.; Lindquist, Y.; Shanklin, J.; Somerville, C.
Preliminary crystallographic data for stearoyl-acyl carrier protein desaturase from castor seed
J. Mol. Biol.
225
561-564
1992
Ricinus communis (P22337)
Manually annotated by BRENDA team
Fox, B.G.; Shanklin, J.; Somerville, C.; Munck, E.
Stearoyl-acyl carrier protein DELTA9 desaturase from Ricinus communis is a diiron-oxo protein
Proc. Natl. Acad. Sci. USA
90
2486-2490
1993
Ricinus communis (P22337), Ricinus communis
Manually annotated by BRENDA team
Cahoon, E.B.; Lindqvist, Y.; Schneider, G.; Shanklin, J.
Redesign of soluble fatty acid desaturases from plants from altered substrate specificity and double bond position
Proc. Natl. Acad. Sci. USA
94
4872-4877
1997
Ricinus communis (P22337)
Manually annotated by BRENDA team
Cahoon, E.B.; Shah, S.; Shanklin, J.; Browse, J.
A determinant of substrate specificity predicted from the acyl-acyl carrier protein desaturase of developing cat's claw seed
Plant Physiol.
117
593-598
1998
Bignonia unguis-cati (O65040), Ricinus communis (P22337)
Manually annotated by BRENDA team
Broadwater, J.A.; Ai, J.; Loehr, T.M.; Sanders-Loehr, J.; Fox, B.G.
Peroxodiferric intermediate of stearoyl-acyl carrier protein DELTA9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation
Biochemistry
37
14664-14671
1998
Ricinus communis (P22337)
Manually annotated by BRENDA team
Haas, J.A.; Fox, B.G.
Role of hydrophobic partitioning in substrate selectivity and turnover of the ricinus communis stearoyl acyl carrier protein DELTA9 desaturase
Biochemistry
38
12833-12840
1999
Ricinus communis (P22337)
Manually annotated by BRENDA team
Whittle, E.; Shanklin, J.
Engineering D9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor DELTA9-18:0-ACP desaturase
J. Biol. Chem.
276
21500-21505
2001
Ricinus communis (P22337)
Manually annotated by BRENDA team
Rogge, C.E.; Fox, B.G.
Desaturation, chain scission, and register-shift of oxygen-substituted fatty acids during reaction with stearoyl-ACP desaturase
Biochemistry
41
10141-10148
2002
Ricinus communis (P22337)
Manually annotated by BRENDA team
Davydov, R.; Behrouzian, B.; Smoukov, S.; Stubbe, J.; Hoffman, B.M.; Shanklin, J.
Effect of substrate on the diiron(III) site in stearoyl acyl carrier protein DELTA9-desaturase as disclosed by cryoreduction electron paramagnetic resonance/electron nuclear double resonance spectroscopy
Biochemistry
44
1309-1315
2005
Ricinus communis
Manually annotated by BRENDA team
Moche, M.; Shanklin, J.; Ghoshal, A.; Lindqvist, Y.
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme DELTA9 stearoyl-acyl carrier protein desaturase: implications for oxygen activation and catalytic intermediates
J. Biol. Chem.
278
25072-25080
2003
Ricinus communis (P22337), Ricinus communis
Manually annotated by BRENDA team