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1.14.19.22: acyl-lipid omega-6 desaturase (cytochrome b5)

This is an abbreviated version!
For detailed information about acyl-lipid omega-6 desaturase (cytochrome b5), go to the full flat file.

Word Map on EC 1.14.19.22

Reaction

an oleoyl-[glycerolipid]
+ 2 ferrocytochrome b5 +
O2
 + 2 H+ =
a linoleoyl-[glycerolipid]
 + 2 ferricytochrome b5 + 2 H2O

Synonyms

1-acyl-2-oleoyl-sn-glycero-3-phosphocholine DELTA12-desaturase, 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine DELTAl2-desaturase, 18:1-phosphatidylcholine desaturase, acyl-lipid DELTA12-desaturase, BrFAD2-1, CeFAT-2, CtFAD2-1, delta 12 fatty acid desaturase, delta-12 fatty acid desaturase 2, Delta-12 oleate desaturase, delta-twelve fatty acid desaturase 2, DELTA12 desaturase, DELTA12-desaturase, DELTA12-fatty acid desaturase, DELTA12-oleoyl-phosphatidylcholine desaturase, desaturase, oleate, DiFAD2, EC 1.3.1.35, endoplasmic reticulum-localized oleate desaturase, FAD2, FAD2-1, FAD2-1A, FAD2-1B, FAD2-2, FAD2-3, FAD2-4, FAD2A, FAD6, linoleate synthase, LKFAD15, microsomal oleate desaturase, microsomal oleic acid desaturase, microsomal omega-6 fatty acid desaturase, oleate desaturase, oleoyl phosphatidylcholine desaturase, oleoyl-CoA desaturase, oleoyl-PC desaturase, oleoyl-phosphatidylcholine desaturase, oleoylphosphatidylcholine desaturase, omega-6 desaturase, omega-6 fatty acid desaturase, omega-6-oleate desaturase, omega6-fatty acid desaturase, OsFAD2, plastidial oleate desaturase, seed-specific delta-12 fatty acid desaturase 2, SVE1, TauDELTA12des

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
                1.14.19.22 acyl-lipid omega-6 desaturase (cytochrome b5)

Engineering

Engineering on EC 1.14.19.22 - acyl-lipid omega-6 desaturase (cytochrome b5)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A104G
-
2.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/M324V
-
2.6fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/S322A
-
3.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/S322A/M324V
-
4.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I
-
29.5fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/M324V
-
36.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/S322A
-
44.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/S322A/M324V
-
90.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148N/S322A/M324I
-
24.6fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
M324I
-
54.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
M324V
-
49.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
S322A
-
1.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
S322A/M324V
-
2.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I
-
14.8fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/M324V
-
26.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/S322A
-
26.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/S322A/M324V
-
34.4fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148N
-
3.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
D150N
-
the mutation of the ahFAD2 gene results in a dysfunctional desaturase
G374E
-
line 743, missense mutations in a less conserved region, seed phenotype does not differ from wild-type
P137R
-
the PI 283327 FAD2-1B allele, carrying the mutant FAD2-1B P137R allele, is associated with an increase in seed oleic acid content
S117N
S238F
-
line 615, missense mutations in a less conserved region, seed phenotype does not differ from wild-type
additional information
-
mutation Ol greatly increases oleic acid and is correlated with greatly reduced expression of enzyme isoform FAD2-1. FAD2-1 gene is duplicated in Ol mutants. Development of dominant INDEL markers diagnostic for presence or absence of the Ol mutation