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Literature summary for 6.2.1.5 extracted from

  • Hamblin, K.; Standley, D.M.; Rogers, M.B.; Stechmann, A.; Roger, A.J.; Maytum, R.; van der Giezen, M.
    Localization and nucleotide specificity of Blastocystis succinyl-CoA synthetase (2008), Mol. Microbiol., 68, 1395-1405.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.5

Cloned(Commentary)

Cloned (Comment) Organism
alpha and beta subunits, expression of His-tagged proteins in Escherichia coli strain BL21(DE3), phylogenetic analysis of SCS subunits Blastocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme is located in a mitochondrion-like organelle Blastocystis sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Blastocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32500
-
 2 * 32500, alphabeta, SDS-PAGE, 1 * 33400, alpha-subunit, + 1 * 45100, beta-subunit, sequence calculation Blastocystis sp.
33400
-
 2 * 32500, alphabeta, SDS-PAGE, 1 * 33400, alpha-subunit, + 1 * 45100, beta-subunit, sequence calculation Blastocystis sp.
45100
-
 2 * 32500, alphabeta, SDS-PAGE, 1 * 33400, alpha-subunit, + 1 * 45100, beta-subunit, sequence calculation Blastocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate + CoA Blastocystis sp. Blastocystis succinyl-CoA synthetase is a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. In the absence of a classic mitochondrial electron transport chain, it is likely to be one of the main ATP producing enzymes in this parasite ADP + phosphate + acetyl-CoA
-
 r

Organism

Organism UniProt Comment Textmining
Blastocystis sp.
-
 human isolate, strain DMP/02-328, ATCC 50177
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged proteins from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Blastocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA Blastocystis succinyl-CoA synthetase is a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. In the absence of a classic mitochondrial electron transport chain, it is likely to be one of the main ATP producing enzymes in this parasite Blastocystis sp. ADP + phosphate + acetyl-CoA
-
 r
ATP + acetate + CoA Blastocystis SCS is ATP-specific, while both ATP and GTP fit into the Blastocystis SCS active site, GTP is destabilizes by electrostatic dipole interactions with Lys42 and Lys110, the side-chains of which lie outside the nucleotide-binding cavity, an electrostatic gatekeeper controls which ligands can enter the binding site, overview Blastocystis sp. ADP + phosphate + acetyl-CoA three reaction steps in the reverse direction: 1. formation of a non-covalent enzyme-succinyl-phosphate complex and cocomitant release of CoA, 2. formation of a covalent phosphoryl-enzyme intermediate with the release of succinate, and 3. phosphorylation of ADP forming ATP r

Subunits

Subunits Comment Organism
dimer 2 * 32500, alphabeta, SDS-PAGE, 1 * 33400, alpha-subunit, + 1 * 45100, beta-subunit, sequence calculation Blastocystis sp.
More homology modelling using pig SCS, PDB code 2fp4, induced-fit docking calculations and molecular dynamics simulations, overview Blastocystis sp.

Synonyms

Synonyms Comment Organism
SCS
-
 Blastocystis sp.
Succinyl-CoA synthetase
-
 Blastocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Blastocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Blastocystis sp.

Cofactor

Cofactor Comment Organism Structure
ATP specific for, while both ATP and GTP fit into the Blastocystis SCS active site, GTP is destabilized by electrostatic dipole interactions with Lys42 and Lys110, the side-chains of which lie outside the nucleotide-binding cavity, flexible docking and molecular dynamics simulations, overview Blastocystis sp.

pI Value

Organism Comment pI Value Maximum pI Value
Blastocystis sp. beta-subunit, sequence calculation
-
 8.47
Blastocystis sp. alpha-subunit, sequence calculation
-
 9.34