Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.79 recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21/DE3 Synechococcus sp. PCC 7002

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.79 purified recombinant His6-tagged wild-type Sp2771, and Sp2771 S419A and Sp2771 C262A mutants in ternary complex with NADP+ and succinate semialdehyde, mixing of 0.001 ml of protein solution and reservoir solution each, the latter containing 15% PEG 5000 MME , 1 mM DTT, 3% tascimate, and 100 mM HEPES, pH 6.8 for the wild-type enzyme and the mutants, for Sp2771 mutants in complex with NADP+ and succinate semialdehyde, NAD+ and succinate semialdehyde are incubated with proteins for 15 min at room temperature before crystallization, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement using Escherichia coli SSADH structure, PDB ID 3JZ4, as search model Synechococcus sp. PCC 7002

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.79 C262A site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure Synechococcus sp. PCC 7002
1.2.1.79 S419A site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure Synechococcus sp. PCC 7002

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. PCC 7002
-
succinate + NADPH + 2 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.79 Synechococcus sp. PCC 7002 B1XMM6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.79 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration Synechococcus sp. PCC 7002

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.79 succinate semialdehyde + NADP+ + H2O
-
Synechococcus sp. PCC 7002 succinate + NADPH + 2 H+
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.79 More the central parts of both cofactor binding domain and catalytic domain contain atypical alpha/beta structure. The catalytic domain consists of a seven stranded beta-sheet flanked by two alpha-helices on one side and three alpha-helices on the other side.The cofactor binding domain displays the two tandem Rossmann folds for NADP+ binding . The oligomerization domain contains three-stranded antiparallel beta-sheets protruding across the center of the dimer interface, while the NADP+ binding site is on the opposite side of the dimer interface Synechococcus sp. PCC 7002

Synonyms

EC Number Synonyms Comment Organism
1.2.1.79 Sp2771
-
Synechococcus sp. PCC 7002
1.2.1.79 SSADH
-
Synechococcus sp. PCC 7002
1.2.1.79 succinic semialdehy de dehydrogenase
-
Synechococcus sp. PCC 7002
1.2.1.79 SYNPCC7002_A2771 gene name, UniProt Synechococcus sp. PCC 7002

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.79 22
-
assay at room temperature Synechococcus sp. PCC 7002

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.79 NADP+ Ser157 residue in Sp2771 plays a critical structural role in determining NADP+ preference for Sp2771, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection Synechococcus sp. PCC 7002

General Information

EC Number General Information Comment Organism
1.2.1.79 additional information Ser157 residue in Sp2771 plays a critical structural role in determining NADP+ preference for Sp2771, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Enzyme Sp2771 structure modelling comprising residues 2-454, active site and substrate binding structures, overview Synechococcus sp. PCC 7002