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Literature summary for 1.2.1.79 extracted from

  • Yuan, Z.; Yin, B.; Wei, D.; Yuan, Y.R.
    Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase (2013), J. Struct. Biol., 182, 125-135.
    View publication on PubMed
Search for more literature for 1.2.1.79

Cloned(Commentary)

Cloned (Comment) Organism
insertion of the full length Sp2771 gene into pET28b vector with an N-terminal His-6 tag and expression in Escherichia coli (BL21/DE3) strain Synechococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of wild type Sp2771 at 2.1 A resolution, Sp2771 S419A mutant at 2.5 A resolution and ternary structure of non-catalytic Sp2771 C262A mutant in complex with NADP + and succinate semialdehyde at 1.7 A resolution Synechococcus sp.

Protein Variants

Protein Variants Comment Organism
C262A mutation abolishes catalytic activity, catalytic residue Synechococcus sp.
E228A mutation abolishes catalytic activity, catalytic residue Synechococcus sp.
R139A 90% reduced catalytic activity, residue is involved in substrate binding Synechococcus sp.
S157E mutation changes cofactor preference from NADP+ to NAD+, but enzyme activity is approximately 10fold reduced Synechococcus sp.
S419A 80% reduced catalytic activity, residue is involved in substrate binding Synechococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
91000
-
 analytical ultracentrifugation Synechococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinate semialdehyde + NADP+ + H2O Synechococcus sp.
-
 succinate + NADPH + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Synechococcus sp. B1XMM6
-
-

Purification (Commentary)

Purification (Comment) Organism
through Ni2+ affinity column chromatography, followed by a Hi-Load Superdex S-75 26/60 column chromatography Synechococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinate semialdehyde + NADP+ + H2O
-
 Synechococcus sp. succinate + NADPH + 2 H+
-
 ?

Subunits

Subunits Comment Organism
dimer Sp2771 monomer is composed of N-terminal cofactor binding domain, a catalytic domain and an oligomerization domain Synechococcus sp.

Synonyms

Synonyms Comment Organism
Sp2771
-
 Synechococcus sp.
SSADH
-
 Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
additional information no detectable activity by using NAD+ as cofactor Synechococcus sp.
NADP+ strict preference Synechococcus sp.

General Information

General Information Comment Organism
metabolism Sp2771 enzyme completes together with a novel 2-oxoglutarate decarboxylase a non-canonical tricarboxylic acid cycle Synechococcus sp.