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Literature summary extracted from

  • Langendorf, C.G.; Key, T.L.; Fenalti, G.; Kan, W.T.; Buckle, A.M.; Caradoc-Davies, T.; Tuck, K.L.; Law, R.H.; Whisstock, J.C.
    The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions (2010), PLoS One, 5, e9280.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.2.1.79 medicine analysis of Escherichia coli SSADH structure with respect to human disease-linked mutations Escherichia coli K-12

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.79
-
 Escherichia coli K-12
1.2.1.79 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.79 comparison to human enzyme, analysis of NADP+ binding site. Enzyme is a homotetramer with the 4 monomers related by a non-crystallographic 222 symmetry. The conserved catalytic site residues and active site residues correspond to C288 and E254 as well as R164, R282 and S445, respectively Escherichia coli K-12
1.2.1.79 in complex with NADP+, hanging drop vapour diffusion method, using 0.2 M ammonium tartrate, 26-31% polyethylene glycol 3350, 10 mM beta-mercaptoethanol and 0.1 M Tris (pH 7.2-7.5) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.24 A237S the mutant shows 65% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 C223Y the mutant shows 5% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 C93F the mutant shows 3% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 G176R the mutant shows less than 1% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 G268E the mutant shows less than 1% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 G409D the mutant shows less than 1% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 G46R the mutant shows 87% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 G533R the mutant shows less than 1% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 H180Y the mutant shows 83% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 N255S the mutant shows 17% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 N335K the mutant shows 1% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 P182L the mutant shows 48% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 P382L the mutant shows 2% activity compared to the wild type enzyme Homo sapiens
1.2.1.24 T233M the mutant shows 4% activity compared to the wild type enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.79 0.01694
-
 succinate semialdehyde pH 8.0, 30°C Escherichia coli K-12
1.2.1.79 0.01694
-
 succinate semialdehyde in 100 mM sodium phosphate buffer, pH 8.0, 30°C Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.24 succinate semialdehyde + NAD+ + H2O Homo sapiens
-
 succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NAD+ + H2O Escherichia coli the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NAD+ + H2O Escherichia coli MC1061 the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NADP+ + H2O Escherichia coli the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ succinate + NADPH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NADP+ + H2O Escherichia coli MC1061 the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ succinate + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.24 Homo sapiens P51649
-
-
1.2.1.79 Escherichia coli P25526
-
-
1.2.1.79 Escherichia coli K-12 P25526
-
-
1.2.1.79 Escherichia coli MC1061 P25526
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.79 nickel chelating Sepharose column chromatography and S200 16/60 gel filtration Escherichia coli
1.2.1.79 recombinant enzyme Escherichia coli K-12

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.24 succinate semialdehyde + NAD+ + H2O
-
 Homo sapiens succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NAD+ + H2O the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NAD+ + H2O the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli MC1061 succinate + NADH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NADP+ + H2O the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli succinate + NADPH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NADP+ + H2O the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli MC1061 succinate + NADPH + H+
-
 ?
1.2.1.79 succinate semialdehyde + NADP+ + H2O
-
 Escherichia coli K-12 succinate + NADPH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.79 tetramer x-ray crystallography Escherichia coli
1.2.1.79 tetramer crystallographic data Escherichia coli K-12

Synonyms

EC Number Synonyms Comment Organism
1.2.1.24 SSADH
-
 Homo sapiens
1.2.1.24 succinic semialdehyde dehydrogenase
-
 Homo sapiens
1.2.1.79 gabD
-
 Escherichia coli K-12
1.2.1.79 SSADH
-
 Escherichia coli
1.2.1.79 SSADH
-
 Escherichia coli K-12
1.2.1.79 succinic semialdehyde dehydrogenase
-
 Escherichia coli
1.2.1.79 succinic semialdehyde dehydrogenase
-
 Escherichia coli K-12

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.24 NAD+
-
 Homo sapiens
1.2.1.79 additional information no cofactor: NAD+ Escherichia coli K-12
1.2.1.79 NAD+ the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli
1.2.1.79 NADP+ electron density analysis of binding site. The enzyme activity measured in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli K-12
1.2.1.79 NADP+ the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli

General Information

EC Number General Information Comment Organism
1.2.1.24 metabolism SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid Homo sapiens
1.2.1.79 metabolism SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid Escherichia coli