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Literature summary for 6.2.1.5 extracted from

  • Bishop, D.F.; Tchaikovskii, V.; Hoffbrand, A.V.; Fraser, M.E.; Margolis, S.
    X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2) (2012), J. Biol. Chem., 287, 28943-28955.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
molecular biology the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, bound to an amylose resin, is used as an affinity ligand to bind FPLC-purified wild-type and some mutant erythroid-specific aminolevulinic acid synthases, ALAS2 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, in Escherichia coli strain Top10 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Homo sapiens 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9P2R7 beta-subunit
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Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, from Escherichia coli strain Top10 by amylose affinity chromatography and gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythroid cell
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Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Succinyl-CoA synthetase
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Homo sapiens
SUCLA2
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Homo sapiens

General Information

General Information Comment Organism
additional information C-terminal mutations in the erythroid-specific aminolevulinic acid synthase gene ALAS2 cause loss of binding to the beta-subunit of succinyl-CoA synthetase, SUCLA2, resulting in reduced mitochondrial enzymatic activity and X-linked sideroblastic anemia Homo sapiens
physiological function probable role of an aminolevulinic acid synthase ALAS2-succinyl-CoA synthetase complex in the regulation of erythroid heme biosynthesis Homo sapiens