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

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.19.2
-
RECOMMENDED NAME
GeneOntology No.
stearoyl-[acyl-carrier-protein] 9-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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oleate biosynthesis I (plants)
-
-
palmitoleate biosynthesis II (plants and bacteria)
-
-
arachidonate biosynthesis
-
-
Fatty acid biosynthesis
-
-
Biosynthesis of unsaturated fatty acids
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
milkweed
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bignonia unguis-cati
cat's claw
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
coriander
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
i.e. Millettia pinnata or Cytisus pinnatus
S5U3F4
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cvs. Hojiblanca, Picudo, Manzanilla, Picual and Arbequina
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
avocado
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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
-
?
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
-
?
palmitoyl-[acyl-carrier protein] + AH2 + O2
palmitoleoyl-[acyl-carrier protein] + A + H2O
show the reaction diagram
palmitoyl-[acyl-carrier protein] + reduced acceptor + O2
9-hexadecenoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
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-CoA + electron donor + O2
9-octadecenoyl-CoA + acceptor + H2O
show the reaction diagram
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
stearoyl-[acyl-carrier protein] + electron donor + O2
oleoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + electron donor + O2
oleoyl-[acyl-carrier protein] + electron acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + ferredoxin + O2
oleoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
stearoyl-[acyl-carrier protein] + reduced acceptor + O2
9-octadecenoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + reduced acceptor + O2
oleoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
oleoyl-[acyl-carrier protein] + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
stearoyl-[acyl-carrier-protein] + reduced acceptor + O2
oleoyl-[acyl-carrier-protein] + acceptor + H2O
show the reaction diagram
tetradecanoyl-[acyl-carrier protein] + reduced acceptor + O2
9-tetradecenoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
stearoyl-[acyl-carrier protein] + electron donor + O2
oleoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + electron donor + O2
oleoyl-[acyl-carrier protein] + electron acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + ferredoxin + O2
oleoyl-[acyl-carrier protein] + oxidized ferredoxin + H2O
show the reaction diagram
Q4JIJ4
-
-
-
?
stearoyl-[acyl-carrier protein] + reduced acceptor + O2
oleoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
oleoyl-[acyl-carrier protein] + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
stearoyl-[acyl-carrier-protein] + reduced acceptor + O2
oleoyl-[acyl-carrier-protein] + acceptor + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
NADPH
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-mercaptoethanol
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cytochrome c3
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cytochrome c553
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-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
catalase
-
dithiothreitol
enhances activity
reduced glutathione
enhances activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0074
10-(heptyloxy)-decanoyl-[acyl-carrier protein]
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-
0.0066
7-(decyloxy)-heptanoyl-[acyl-carrier protein]
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-
0.0059
heptadecanoyl-[acyl-carrier protein]
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-
0.00055 - 0.0083
hexadecanoyl-[acyl-carrier protein]
0.0013
nonadecanoyl-[acyl-carrier protein]
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-
0.00046 - 0.0039
octadecanoyl-[acyl-carrier protein]
0.00051
palmitoyl-[acyl-carrier protein]
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-
0.069
pentadecanoyl-[acyl-carrier protein]
-
-
0.0083
stearoyl-CoA
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-
0.00038
stearoyl-[acyl-carrier protein]
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-
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]
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-
0.2
7-(decyloxy)-heptanoyl-[acyl-carrier protein]
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-
0.04
8-(nonyloxy)-octanoyl-[acyl-carrier protein]
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-
0.02
9-(octyloxy)-nonanoyl-[acyl-carrier protein]
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-
0.233
heptadecanoyl-[acyl-carrier protein]
-
-
0.0467 - 0.422
hexadecanoyl-[acyl-carrier protein]
0.2
nonadecanoyl-[acyl-carrier protein]
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-
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]
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000016
activity in extracts from Escherichia coli M15 transformed with pQESAD, uninduced, with reduced spinach ferredoxin
0.000002
activity in extracts from Escherichia coli M15 transformed with pQESAD, uninduced, without reduced spinach ferredoxin
0.000003
His-tag fusion protein overexpressed in Escherichia coli M15 without ferredoxin, without IPTG-induction
0.0000075
activity in extracts from Escherichia coli M15 transformed with pQESAD, induced, with reduced spinach ferredoxin
0.000079
activity in extracts from Escherichia coli M15 transformed with pQESAD, induced, without reduced spinach ferredoxin
0.000082
His-tag fusion protein overexpressed in Escherichia coli M15 without ferredoxin, IPTG-induced
0.00157
His-tag fusion protein overexpressed in Escherichia coli M15 with exogenous spinach ferredoxin, without IPTG-induction
0.00795
His-tag fusion protein overexpressed in Escherichia coli M15 with exogenous spinach ferredoxin, without IPTG-induced
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.7
-
pH 5.5: about 50% activity, pH 7.7: about 50% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.34
sequence calculation
6.4
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low enzyme content
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
RT-PCR, gene-specific primers for the isoform; RT-PCR, gene-specific primers for the isoform; RT-PCR, gene-specific primers for the isoform; RT-PCR, gene-specific primers for the isoform; RT-PCR, gene-specific primers for the isoform; RT-PCR, gene-specific primers for the isoform
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
2 * 36000, SDS-PAGE
37000
-
alpha2, 2 * 37000, recombinant enzyme lacking a putative transit peptide, SDS-PAGE
39000
-
x * 39000, recombinant enzyme, SDS-PAGE, predicted from nucleotide sequence
43000
SDS-PAGE, overexpressed His-tag fusion protein
43500
recombinant 6 x His-SAD, determined by SDS-PAGE
44180
calculated from amino acid sequence
45020
calculated from amino acid sequence
45290
calculated from amino acid sequence
45480
calculated from amino acid sequence
45510
precursor
45690
calculated from amino acid sequence
45860
calculated from amino acid sequence
46000
-
x * 46000, SDS-PAGE
46950
calculated from amino acid sequence
47040
x * 47040, calculated from amino acid sequence
49000
-
x * 49000, isoform 2, SDS-PAGE
50500
-
determined by SDS-PAGE
68000
-
gel filtration
75000
-
recombinant enzyme lacking a putative transit peptide
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DesA2 crystals grown by the method of hanging drop vapor diffusion, one metal bound per subunit which is likely Mn2+, native and selenomethionine-substituted, 2.0 A resolution X-ray structure
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
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in complex with azide or acetae, apo- and single-iron form
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
1 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to dialysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 50% glycerol, 0.1% bovine serum albumin, 100 mM potassium phosphate buffer, pH 6.8, at least 2 months, no loss of activity
-
0C, 10 h, 50% loss of activity
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4C, overnight, 30% loss of activity
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frozen state, 1 month, complete loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aceton powder, anion-exchange, affinity chromatography on acyl-carrier protein-Sepharose
-
by Ni-NTA purification system
-
DesA2 isoform purified by ion exchange and gel filtration chromatographies
overexpressed S-ACP-DES1 enzyme; overexpressed S-ACP-DES3 enzyme; overexpressed S-ACP-DES4 enzyme; overexpressed S-ACP-DES5 enzyme
recombinant enzyme
recombinant enzyme lacking a putative transit peptide
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a Brassica napus bacterial artificial chromosome, BAC, library is constructed
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cloned in pQE-30 vector and expressed in Escherichia coli strain M15, His-tag
cloning of isoform 1; cloning of isoform 2
DesA1 overexpressed in Escherichia coli BL21-(DE3) with the natural N-terminal methionine residue as the first amino acid; DesA2 overexpressed in Escherichia coli BL21-(DE3) with the natural N-terminal methionine residue as the first amino acid
expressed in Escherichia coli BL21 Star (DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of 2 isoforms in Escherichia coli
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expression of cDNA in Escherichia coli
full-length cDNA clone
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gene CocoFAD, isolated from a cDNA library prepared from the endosperm of coconut, DNA and amino acid sequence determmination and analysis, sequence comparisons and phylogenetic analysis and tree, real-time fluorescent quantitative PCR expresion analysis, recombinant expression in Saccharomyces cerevisiae strain INVSc1, the levels of palmitoleic acid (16:1) and oleic acid (18:1) are improved significantly, stearic acid (18:0) is reduced in recombinant cells
gene FAB2, real-time quantitative PCR enzyme expression analysis
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gene FAB2, sequence comparisons, semi-quantitative RT-PCR expression analysis, recombinant overexpression in Chlamydomonas reinhardtii
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gene Gmsacpd-c, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
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gene NbSACPD-A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; gene NbSACPD-B, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; gene NbSACPD-C, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene sad, cloning from embryo, DNA and amino acid sequence determination and analysis, quantitative and semi-quantitative real-time RT-PCR enzyme expression analysis, recombinant XsSAD expression in Escherichia coli cells resulting in increased 18:1D9 level, and confirming the biological activity of the enzyme encoded by XsSAD. Recombinant XsSAD expression in and partial complementation of Arabidopsis thaliana ssi2 mutant, via Agrobacterium strain GV3101 transformation method,control of 35S promoter partially restors the morphological phenotype and effectively increases the 18:1D9 level. The levels of other unsaturated fatty acids synthesized with 18:1D9 as the substrate also increase to some degree
gene SAD, DNA and amino acid sequence determination and analysis, enzyme expressioon analysis
gene SAD, DNA and amino acid sequence determination and analysis, ZmSAD1-based association mapping, genotyping, sequence comparisons, phylogenetic analysis, quantitative reverse transcription PCR enzyme expression analysis
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gene sad, multiple copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
S5U3F4
gene SAD1, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD2, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD3, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD4, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD5, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD6, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, recombinant expression in Arabidopsis thaliana homozygous fab2 mutant, ssi2 mutant background, driven by CaMV 35S promoter; gene SAD7, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis, SAD7 cannot be recombinantly expressed in Arabidopsis thaliana; gene SAD8, cloned from leaves, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR isozyme expression analysis
gene SAD1, cloning of the isozyme from Olea europaea cv. Picual, DNA and amino acid sequence determination and analysis, isozyme sequence comparison and phylogenetic analysis, expression analysis; gene SAD2, cloning of the isozyme from Olea europaea cv. Picual, DNA and amino acid sequence determination and analysis, isozyme sequence comparison and phylogenetic analysis, expression analysis; gene SAD3, cloning of the isozyme from Olea europaea cv. Picual, DNA and amino acid sequence determination and analysis, isozyme sequence comparison and phylogenetic analysis, expression analysis
gene SAD1, phylogenetic analysis
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gene SAD1, phylogenetic analysis, ZmSAD1 overexpression (ZmSAD1), antisense ZmSAD1 (anti-ZmSAD1), and ZmSAD1 RNA interference (ZmSAD1 RNAi) constructs are generated in the pBI121 vector under control of the seed-specific FAE1 promoter, recombinant expression in Arabidopsis thaliana with higher expression levels in mature seeds and immature siliques than in roots, stems, leaves, and petals. Fatty acid composition and content are modified in the transgenic Arabidopsis seeds, seed-specific overexpression of the exogenous ZmSAD1 gene significantly reduces the content of stearic acid and the ratio of saturated to unsaturated fatty acids, composition of fatty acids in the Arabidopsis seeds harbouring the exogenous ZmSAD1, anti-ZmSAD1, or ZmSAD1 RNAi constructs. Phenotypes, overview
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into the pUCm-T vector and subcloned into the vector pET30a for expression in Escherichia coli BL21DE3 cells
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into the vector pQE-30 for expression in Escherichia coli M15 cells
OeSAD2 is not expressed as a soluble protein
-
S-ACP-DES1 expressed in Escherichia coli; S-ACP-DES3 enzyme expressed in Escherichia coli; S-ACP-DES4 enzyme expressed in Escherichia coli; S-ACP-DES5 enzyme expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
12-24 h after cold stress the enzyme expression is strongly increased and decreases thereafter
-
ahSAD3 is expressed exclusively during seed development
-
at lower temperatures plants and microalgae upregulate the expression of the SAD gene to produce more unsaturated fatty acids to maintain membrane fluidity at lower temperatures
exposure to HL (0.4 mM photons m-2 s-1) significantly increases the enzyme's mRNA level. Nitrogen deficiency also markedly up-regulates the expression of the enzyme. mRNA levels of the enzyme are drastically upregulated, reaching their maximum at 48 h after glucose induction
seed-specific down-regulation of endogenous AtSAD genes in Arabidopsis significantly increases the content of stearic and long-chain saturated fatty acids and the ratio of saturated to unsaturated fatty acids, whereas it significantly decreases the oleic acid content. Composition of fatty acids in the Arabidopsis seeds harbouring the exogenous ZmSAD1, anti-ZmSAD1, or ZmSAD1 RNAi constructs, overview
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the stearoyl-ACP desaturase gene PtSAD is slightly downregulated within the first four hours of heat stress at 35C and upregulated whereafter, and reaches a peak level 48 h later
ENGINEERING
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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mutant strain showing contents of up to 20% of unusual acyl chains such as 16:1DELTA9, 16:2DDELTA9,12, 18:1DELTA11, increase of enzyme activity in mutant
biofuel production
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biodiesel production
biotechnology
-
random mutagenesis and mutational analysis allows for the achievement of high seed stearic acid content with no associated negative agronomic characteristics, raandom mutagenesis as a rheostat for agronomically important traits
Show AA Sequence (168 entries)
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