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1.14.19.2: stearoyl-[acyl-carrier-protein] 9-desaturase

This is an abbreviated version!
For detailed information about stearoyl-[acyl-carrier-protein] 9-desaturase, go to the full flat file.

Word Map on EC 1.14.19.2

Reaction

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

Synonyms

acyl-ACP-desaturase, acyl-[acyl-carrier-protein] desaturase, ahSAD3A, ahSAD3B, AtSAD1, CrFAB2, CSAD, DELTA9 desaturase, DELTA9-stearoyl-ACP-desaturase-C, DesA1, DesA2, desaturase, acyl-[acyl carrier protein], EC 1.14.99.6, FAB, FAB2, Gmsacpd-c, NbSACPD-A, NbSACPD-B, NbSACPD-C, OeSAD2, OeSAD3, OsSAD1, OsSAD2, OsSAD3, PpSAD, PtSAD, S-ACP-DES, S-ACP-DES1, S-ACP-DES2, S-ACP-DES3, S-ACP-DES4, S-ACP-DES5, S-ACP-DES6, SACPD, SACPD-C, SAD, SAD1, SAD2, SAD3, SAD4, SAD6, SAD7, SAD8, SLL1, SSI2 desaturase, SSI2/FAB2, stearoyl-ACP desaturase, stearoyl-acyl carrier protein (ACP) desaturase, stearoyl-acyl carrier protein desaturase, stearoyl-acyl carrier protein desaturase 3, stearoyl-acyl carrier protein desaturase-1, stearoyl-acyl carrier protein fatty acid desaturase, stearoyl-[acyl carrier protein] desaturase, stearyl acyl carrier protein desaturase, stearyl-ACP desaturase, stearyl-acyl carrier protein desaturase, Tc01g009910, Tc04g005590, Tc04g017510, Tc04g017520, Tc04g017540, Tc05g012840, Tc08g012550, Tc09g024040, TcSAD1, TcSAD2, TcSAD3, TcSAD4, TcSAD5, TcSAD6, TcSAD7, TcSAD8, XsSAD, ZmSAD1

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
                1.14.19.2 stearoyl-[acyl-carrier-protein] 9-desaturase

Engineering

Engineering on EC 1.14.19.2 - stearoyl-[acyl-carrier-protein] 9-desaturase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C235T
-
random mutagenesis
C247T
-
random mutagenesis
C305T
-
random mutagenesis
D77N
-
random mutagenesis, the alteration of charge in the missense mutants SACPD-CD77N is due to the iron ion pocket localization, the mutation is predicted to affect iron ion-binding kinetics and stability
E114K
-
random mutagenesis, the mutation directly alters the negatively charged bridging ligand Glu114 into a positively charged Lys
G1777A
-
random mutagenesis
G1964T
-
random mutagenesis
G229A
-
random mutagenesis
G340A
-
random mutagenesis
L79F
-
random mutagenesis, the alteration of charge in the missense mutants SACPD-CD77N is due to the iron ion pocket localization, presence of steric hindrance by L79F, the mutation is predicted to affect iron ion-binding kinetics and stability
P102L
-
random mutagenesis, the missense mutant SACPD-CP102L is not localized at the iron ion-binding pocket but is positioned at the first residue of the alpha4 chain,which holds the ligands Glu114 and His117 in place. Considering Pro's cyclic conformation, in which the secondary amine binds to the alha-carbon of the protein backbone, a disruption of this conformational rigidity may impact the ability of the alpha4 chain to be in its proper location, disrupting the enzymatic activity of GmSACPD-C
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
additional information