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Literature summary for 2.5.1.47 extracted from

  • Feldman-Salit, A.; Wirtz, M.; Hell, R.; Wade, R.C.
    A mechanistic model of the cysteine synthase complex (2009), J. Mol. Biol., 386, 37-59.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
construction of a model of the cysteine synthase complex composed of the enzymes serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL. Binding energy calculations suggest that, consistent with experiments, a ratio of two OAS-TL dimers to one SAT hexamer is likely Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place Escherichia coli
additional information upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Escherichia coli 5739
-
mitochondrion
-
Arabidopsis thaliana 5739
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P47998
-
-
Escherichia coli P16703
-
-