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Literature summary extracted from

  • Park, J.; Rhee, S.
    Structural basis for a cofactor-dependent oxidation protection and catalysis of cyanobacterial succinic semialdehyde dehydrogenase (2013), J. Biol. Chem., 288, 15760-15770.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.79 N-terminal His-tagged SySSADH expressed in Escherichia coli B834 (DE3) methionine auxotroph cells Synechococcus sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.79 crystal structures of SySSADH determined in their apo form, as a binary complex with NADP+ and as a ternary complex with succinic semialdehyde and NADPH, resoultion of 1.7 A for the apo form and of 1.4 A for the binary and ternary complex Synechococcus sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.79 C262A active site mutation, nonfunctional because Cys-262 acts as a nucleophilel Synechococcus sp.
1.2.1.79 E228A active site mutation, nonfunctional because Glu-228 acts as a general base Synechococcus sp.
1.2.1.79 E228Q active site mutation, nonfunctional because Glu-228 acts as a general base Synechococcus sp.
1.2.1.79 F132A activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity Synechococcus sp.
1.2.1.79 F425A inactive, suggesting that Phe-425 plays an important role in substrate binding Synechococcus sp.
1.2.1.79 I263A activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity Synechococcus sp.
1.2.1.79 N131A mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity Synechococcus sp.
1.2.1.79 N131D mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity Synechococcus sp.
1.2.1.79 R139A activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity Synechococcus sp.
1.2.1.79 R139K mutant enzyme exhibited an activity up to 80% that of the wild type enzyme, suggesting the significance of a positively charged residue in the binding of the carboxyl group of succinic semialdehyde Synechococcus sp.
1.2.1.79 S419A mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity Synechococcus sp.
1.2.1.79 W135A activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity Synechococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.79 H2O2 50 microM H2O2 sharply reduces activity to 31% of the H2O2-free enzyme and activity further decreases to 3% at 1 mM H2O2 Synechococcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.79 additional information
-
 additional information the Km-value of succinate semialdehyde estimated to be far less than 0.05 mM Synechococcus sp.
1.2.1.79 0.439
-
 NADP+ 30°C, pH 7.6 Synechococcus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.79 succinate semialdehyde + NADP+ + H2O Synechococcus sp. data from crystal structures provide details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex succinate + NADPH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.79 Synechococcus sp. B1XMM6
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.2.1.79 SySSADH is an oxidation-sensitive enzyme and the formation of the NADP-cysteine adduct is a kinetically preferred event that protects the catalytic Cys-262 from H2O2-dependent oxidative stress Synechococcus sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.79 using immobilized metal affinity chromatography, removal of N-terminal His tag, further purification by immobilized metal affinity chromatography and gel filtration using a Superdex 200 column Synechococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.79 succinate semialdehyde + NADP+ + H2O data from crystal structures provide details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex Synechococcus sp. succinate + NADPH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.79 homodimer gel filtration, SySSADH monomer consists of three segments - alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, and three antiparallel beta-strands constituting a dimerization domain Synechococcus sp.

Synonyms

EC Number Synonyms Comment Organism
1.2.1.79 SSADH
-
 Synechococcus sp.
1.2.1.79 SySSADH
-
 Synechococcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.79 5
-
 NADP+ 30°C, pH 7.6 Synechococcus sp.

General Information

EC Number General Information Comment Organism
1.2.1.79 metabolism succinic semialdehyde dehydrogenase from Synechococcus is an essential enzyme in the tricarboxylic acid cycle of cyanobacteria Synechococcus sp.