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

EC NUMBER
COMMENTARY hide
1.1.1.B47
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
succinate semialdehyde reductase (NADPH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CO2 fixation in Crenarchaeota
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoate:NADP+ oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
show the reaction diagram
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
show the reaction diagram
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
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?
additional information
?
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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
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
show the reaction diagram
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
Q9LSV0
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?
additional information
?
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Q9LSV0
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
recombinant AtGLYR1 prefers NADPH over NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the enzyme contains 1.9 mol of zinc per mol of enzyme monomer
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
NADH
65°C, pH 7.9
0.0022 - 0.006
NADPH
0.052
succinate semialdehyde
65°C, pH 7.9, cosubstrate: NADPH
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
440
NADPH
65°C, pH 7.9
440
succinate semialdehyde
65°C, pH 7.9
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.15
cell extract, NADH-dependent reaction, 65°C, pH 7.9
1.4
cell extract, NADPH-dependent reaction, 65°C, pH 7.9
700
purified enzyme, NADPH-dependent reaction, 65°C, pH 7.9
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
at 65°C, half-maximal activity at pH 6.5 and at pH 8.0
6.9 - 8.4
at 20°C, half-maximal activity at pH 6.9 and at pH 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
2 * 40000, SDS-PAGE
74000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
enzyme domain structure analysis, overview
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
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli Rosetta 2(DE3)
gene GLYR1, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D239A
site-directed mutagenesis
F231A
site-directed mutagenesis
K170A
site-directed mutagenesis, catalytically inactive mutant
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
N174A
site-directed mutagenesis
S121A
site-directed mutagenesis
T95A
site-directed mutagenesis