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 (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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
91000 | - |
analytical ultracentrifugation | Synechococcus sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate semialdehyde + NADP+ + H2O | Synechococcus sp. | - |
succinate + NADPH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechococcus sp. | B1XMM6 | - |
- |
Purification (Comment) | Organism |
---|---|
through Ni2+ affinity column chromatography, followed by a Hi-Load Superdex S-75 26/60 column chromatography | Synechococcus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate semialdehyde + NADP+ + H2O | - |
Synechococcus sp. | succinate + NADPH + 2 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | Sp2771 monomer is composed of N-terminal cofactor binding domain, a catalytic domain and an oligomerization domain | Synechococcus sp. |
Synonyms | Comment | Organism |
---|---|---|
Sp2771 | - |
Synechococcus sp. |
SSADH | - |
Synechococcus sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no detectable activity by using NAD+ as cofactor | Synechococcus sp. | |
NADP+ | strict preference | Synechococcus sp. |
General Information | Comment | Organism |
---|---|---|
metabolism | Sp2771 enzyme completes together with a novel 2-oxoglutarate decarboxylase a non-canonical tricarboxylic acid cycle | Synechococcus sp. |