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Literature summary for 2.5.1.47 extracted from

  • Feldman-Salit, A.; Wirtz, M.; Lenherr, E.D.; Throm, C.; Hothorn, M.; Scheffzek, K.; Hell, R.; Wade, R.C.
    Allosterically gated enzyme dynamics in the cysteine synthase complex regulate cysteine biosynthesis in Arabidopsis thaliana (2012), Structure, 20, 292-302.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Arabidopsis thaliana 5829
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mitochondrion
-
Arabidopsis thaliana 5739
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

General Information

General Information Comment Organism
physiological function the enzyme's active site has two access sites. Binding of the enzyme to the C-terminal tail of serine O-acetyltransferase leads to loss of activity due to reduction in ligand accessibility of the second, unoccupied active site. The observed dynamics of the gates show allosteric closure of the unoccupied active site of the enzyme in the cysteine synthase complex, which can hinder substrate binding, abolishing its turnover to cysteine Arabidopsis thaliana