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Literature summary for 1.2.1.79 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
Search for more literature for 1.2.1.79

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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+
-
 ?
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+
-
 ?
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+
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli P25526
-
-
Escherichia coli K-12 P25526
-
-
Escherichia coli MC1061 P25526
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?
succinate semialdehyde + NADP+ + H2O
-
 Escherichia coli K-12 succinate + NADPH + 2 H+
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
gabD
-
 Escherichia coli K-12
SSADH
-
 Escherichia coli
SSADH
-
 Escherichia coli K-12
succinic semialdehyde dehydrogenase
-
 Escherichia coli
succinic semialdehyde dehydrogenase
-
 Escherichia coli K-12

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor: NAD+ Escherichia coli K-12
NAD+ the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+ Escherichia coli
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
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

General Information Comment Organism
metabolism SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid Escherichia coli