Information on EC 1.2.1.76 - succinate-semialdehyde dehydrogenase (acylating)

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

EC NUMBER
COMMENTARY hide
1.2.1.76
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RECOMMENDED NAME
GeneOntology No.
succinate-semialdehyde dehydrogenase (acylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinate semialdehyde + CoA + NADP+ = succinyl-CoA + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate/4-hydroxybutanate cycle
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crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered)
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succinate fermentation to butanoate
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CO2 fixation in Crenarchaeota
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Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating)
Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde. The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation [1], and in Metallosphaera sedula, where it participates in the 3-hydroxypropanonate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
CAS REGISTRY NUMBER
COMMENTARY hide
56093-26-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
caproaldehyde + coenzyme A + NADP+
n-hexanoyl-CoA + NADPH + H+
show the reaction diagram
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at 8.6% of the rate with succinate-semialdehyde
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r
glutaryl-CoA + NADPH + H+
? + coenzyme A + NADP+
show the reaction diagram
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at 6.7% of the rate with succinyl-coA
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r
glycolaldehyde + coenzyme A + NADP+
? + NADPH + H+
show the reaction diagram
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at 9.1% of the rate with succinate-semialdehyde
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r
n-butyraldehyde + coenzyme A + NADP+
n-butyryl-CoA + NADPH + H+
show the reaction diagram
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at 1% of the rate with succinate-semialdehyde
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r
n-hexanoyl-CoA + NADPH + H+
caproaldehyde + coenzyme A + NADP+
show the reaction diagram
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at 8.1% of the rate with succinyl-coA
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r
palmitoyl-CoA + NADPH + H+
? + coenzyme A + NADP+
show the reaction diagram
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at 15.1% of the rate with succinyl-coA
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r
succinate-semialdehyde + coenzyme A + NADP+
succinyl-CoA + NADPH + H+
show the reaction diagram
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r
succinyl-CoA + NADPH + H+
succinate-semialdehyde + coenzyme A + NADP+
show the reaction diagram
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r
valeraldehyde + coenzyme A + NADP+
n-valeryl-CoA + NADPH + H+
show the reaction diagram
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at 6.0% of the rate with succinate-semialdehyde
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r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
coenzyme A
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pH 8.5, 30°C
4
NADP+
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pH 8.5, 30°C
4.3
NADPH
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pH 7.0, 30°C
2.7
Succinate-semialdehyde
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pH 8.5, 30°C
3.2
succinyl-CoA
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pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41.4
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pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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reduction of succinyl-CoA
8.5
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oxidation of succinate-semialdehyde
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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2 * 55000, SDS-PAGE
115000
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sucrose gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 55000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is air-sensitive. Exposure to air at room temperature or 4°C results in a complete inactivation within 6 h or 24 h, respectively
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
extracts of autotrophically grown cells exhibit an NADPH-dependent succinyl-CoA reductase activity of 200 nM/min*mg of soluble protein, whereas extracts of heterotrophically grown cells exhibit an activity of 10 nM/min*mg of protein
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