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

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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
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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].
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CAS REGISTRY NUMBER
COMMENTARY hide
56093-26-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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B1YBY5
UniProt
Manually annotated by BRENDA team
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B1YBY5
UniProt
Manually annotated by BRENDA team
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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
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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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41.4
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pH 7.0, 30°C
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
B1YBY5;
assay at
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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2 * 55000, SDS-PAGE
115000
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sucrose gradient centrifugation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 55000, SDS-PAGE
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
B1YBY5;
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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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Show AA Sequence (176 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.76)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)