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Information on EC 1.1.1.B47 - succinate semialdehyde reductase (NADPH)
for references in articles please use BRENDA:EC1.1.1.B47
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.B47 succinate semialdehyde reductase (NADPH)
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
- 1.1.1.B47
- gamma-hydroxybutyrate
-
ssars
-
aldo-keto
- sulfurreducens
- gaba-t
- geobacter
- 4-hydroxybutyrate
showSynonyms
succinic semialdehyde reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Msed_1424
succinate semialdehyde reductase
succinic semialdehyde reductase
succinic semialdehyde reductase (NADPH)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
the enzyme performs an acid/base catalytic mechanism involving Lys170 as the general acid and a conserved active-site water molecule
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoate:NADP+ oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
Substrates: very low activity with NADH
Products: -
Products: -
?
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
Substrates: very low activity with NADH
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, the enzyme has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
Products: -
Products: -
?
additional information
?
-
Substrates: malonic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: malonic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: malonic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, the enzyme has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the enzyme contains 1.9 mol of zinc per mol of enzyme monomer
additional information
additional information
no stimulation by Mg2+ or Mn2+ (below 5 mM), or Fe2+ (below 1 mM)
additional information
-
no stimulation by Mg2+ or Mn2+ (below 5 mM), or Fe2+ (below 1 mM)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by malonic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde. Incubation with 10 mM EDTA for 16 h or with 100 mM EDTA for 1 h at temperatures up to 65°C does not inactivate the enzyme, nor does addition of 10 mM EDTA to the assay mixture inhibit enzyme activity
-
additional information
-
no inhibition by malonic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde. Incubation with 10 mM EDTA for 16 h or with 100 mM EDTA for 1 h at temperatures up to 65°C does not inactivate the enzyme, nor does addition of 10 mM EDTA to the assay mixture inhibit enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Seizures
The altered expression of GABA shunt enzymes in the gerbil hippocampus before and after seizure generation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.87
Succinic semialdehyde
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
additional information
additional information
Michaelis-Menten kinetics, the activities of the mutant enzymes with succinic semialdehyde are generally too low for kinetic studies
-
0.0022
NADPH
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.6
Succinic semialdehyde
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 8.4
at 20°C, half-maximal activity at pH 6.9 and at pH 8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
no activity in heterotrophically-grown cell
brenda
-
no activity in heterotrophically-grown cell
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview
metabolism
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis
metabolism
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
metabolism
-
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUCD_METS5
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
360
0
37879
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
enzyme domain structure analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K170E
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170H
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170R
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GLYR1, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kockelkorn, D.; Fuchs, G.
Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: Enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales
J. Bacteriol.
191
6352-6362
2009
Metallosphaera sedula (A4YGN0), Metallosphaera sedula, Metallosphaera sedula DSM 5348 (A4YGN0)
brenda
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Arabidopsis thaliana (Q9LSV0)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.B47)
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Release 2023.1 (January 2023)
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