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Information on EC 1.14.19.1 - stearoyl-CoA 9-desaturase
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1.14.19.1 stearoyl-CoA 9-desaturaseIUBMB Comments
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2).
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Word Map
- 1.14.19.1
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sickle
- cardiac
- children
- ventricular
- pain
- hemoglobin
- arrhythmia
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vaso-occlusive
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transfusion
- anemia
- infarct
- cardiomyopathy
- episode
- cardiovascular
- coronary
- myocardial
- artery
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stratification
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polyunsaturated
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ejection
- hydroxyurea
- stroke
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monounsaturated
- crises
- chest
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defibrillator
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desaturation
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lipogenesis
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arrhythmogenic
- tachycardia
- hemoglobinopathy
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all-cause
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cardioverter
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pufas
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cardioverter-defibrillator
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desaturases
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electrocardiogram
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lipogenic
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transfused
- pharmacology
- thalassemia
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12-lead
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palmitoleic
- agriculture
- tachyarrhythmias
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caregiver
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out-of-hospital
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resynchronization
- medicine
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transcranial
- syncope
- drug development
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holter
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alloimmunization
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
scd, stearoyl-coa desaturase, fatty acid desaturase, scd-1, stearoyl-coa desaturase 1, stearoyl-coa desaturase-1, stearoyl coa desaturase, stearoyl-coenzyme a desaturase, delta9-desaturase, delta9 desaturase, 
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topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cold exposure leads to an induced activity, in vivo cooling causes an activity induction of up to 15 to 30fold. Increase of desaturase synthesis by means of activated gene transcription. Transfer of cells to 10°C causes a smaller increase in activity compared to cells maintained at 30°C
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
regioselectivity, substrate specificity, probably extra-plastidal
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the reducing equivalents required for the desaturation site seem to be supplied from NADPH via cytochrome b5 as electron carrier
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
existence of three highly homologous isoforms: SCD1, SCD2 and SCD3 which show different substrate specificities, here SCD1 is mainly analysed
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of two desaturase genes, isomers CDS1 and CDS2. Cooling treatment of carp causes significant changes to the activity of the DELTA9-desaturase. Modest cooling of carp shows an increase in acticity without any increase in the amount of desaturase protein, suggesting the activation of the pre-existing inactive latent enzyme, possibly by a post-translational mechanism
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
increase of activity induced by cold is preceded by the activation of latent desaturase, probably by a posttranslational mechanism. Amounts of desaturase transcript are increased as a result of cold-induced gene transcription
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
SSI2 gene encodes a member of a family of soluble fatty acid desaturases
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. Formerly EC 1.14.99.5
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
arginyl and tyrosyl residues expected in the active site of enzyme
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
introduction of double bonds at fixed positions from the carboxyl group of the fatty acid. D-hydrogen atoms are removed during desaturation. Mixed-function oxidase, acting via hydroxy acid intermediates. Acetyl-CoA desaturase, carboxylase and fatty acid synthetase are all controlled together as a unit and influenced by dietary components
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the synthesis is transcriptionally regulated by fat-free diet and sterols. Cholesterol-supplemented media as well as the transient transfection induces the expression of stearoyl-CoA desaturase RNA
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the synthesis is transcriptionally regulated by fat-free diet and sterols. Cholesterol-supplemented media as well as the transient transfection induces the expression of stearoyl-CoA desaturase RNA
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
it is suggested that in HepG2 cells the trans-10,cis-12 conjugated linoleic acid isomer regulates human desaturase activity mainly by a posttranslational mechanism
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
isolation of a third fatty acid DELTA9-desaturase. Higher activity with longer chain fatty acid substrates. Desaturase expression is induced significantly by increasing the ratio of carbon to nitrogen
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
multienzyme, insertion of a double bond in 9,10 position
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
incorporation of fatty acid into phospholipid. Enzyme may contain an essential thiol group. Endogenous saturated phospholipid is desaturated rapidly in all experiments in contrast with exogenous saturated phospholipid, which generally is not desaturated
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of an unusual microsomal electron transport system associated with the desaturase
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
significant amounts of DELTA8-isomers are present
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
electron flow from NADH to cytochrome b5, via cytochrome b5 reductase. Different types of acyl-CoA desaturation show immunological differences
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
introduction of double bond at position 9
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the DELTA9-desaturase SCD-1 introduces a cis-double bond into saturated fatty acids between carbons 9 and 10. Preferred substrates of SCD-1 are long-chain acyl-CoAs with 13 to 19 carbons, among them stearoyl-CoA and palmitoyl-CoA, the most abundant saturated fatty acid-CoA ester in mammalians. Dehydrogenation of the pro-R hydrogens at C9 and C10 requires molecular oxygen which is activated at the di-iron center and reduced to water. Two of the electrons transferred to molecular oxygen derive from the acyl-CoA substrate and two others from the di-iron center. The ferrous catalytic center is regenerated by electron transfer from cytochrome b5, which has been suggested to bind to a groove at the cytoplasmic domain and to transmit electrons via two histidine residues (H157 and H298) bridging the distance. Ferrocytochrome b5 is provided by cytochrome b5 reductase using NAD(P)H as co-substrate
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the DELTA9-desaturase SCD-1 introduces a cis-double bond into saturated fatty acids between carbons 9 and 10. Preferred substrates of SCD-1 are long-chain acyl-CoAs with 13 to 19 carbons, among them stearoyl-CoA and palmitoyl-CoA, the most abundant saturated fatty acid-CoA ester in mammalians. Dehydrogenation of the pro-R hydrogens at C9 and C10 requires molecular oxygen which is activated at the di-iron center and reduced to water. Two of the electrons transferred to molecular oxygen derive from the acyl-CoA substrate and two others from the di-iron center. The ferrous catalytic center is regenerated by electron transfer from cytochrome b5, which has been suggested to bind to a groove at the cytoplasmic domain and to transmit electrons via two histidine residues bridging the distance. Ferrocytochrome b5 is provided by cytochrome b5 reductase using NAD(P)H as co-substrate
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of two desaturase genes, isomers CDS1 and CDS2. Cooling treatment of carp causes significant changes to the activity of the DELTA9-desaturase. Modest cooling of carp shows an increase in acticity without any increase in the amount of desaturase protein, suggesting the activation of the pre-existing inactive latent enzyme, possibly by a post-translational mechanism
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cold exposure leads to an induced activity, in vivo cooling causes an activity induction of up to 15 to 30fold. Increase of desaturase synthesis by means of activated gene transcription. Transfer of cells to 10°C causes a smaller increase in activity compared to cells maintained at 30°C
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
isolation of a third fatty acid DELTA9-desaturase. Higher activity with longer chain fatty acid substrates. Desaturase expression is induced significantly by increasing the ratio of carbon to nitrogen
Mortierella alpina CBS 528.72 / ATCC 32222
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PATHWAY SOURCE
PATHWAYS
BRENDA