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Literature summary for 3.4.21.81 extracted from

  • Butala, M.; Zgur-Bertok, D.; Busby, S.J.
    The bacterial LexA transcriptional repressor (2009), Cell. Mol. Life Sci., 66, 82-93.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
native crystal structures at pH 4.2 at a resolution of 1.18 A, and at pH 7.3 at a resolution of 1.23 A. At pH 4.2 the enzyme is assigned as a tetrapeptide, Asp-Ala-Ile-Tyr, whereas at pH 7.3 it is assigned as a tyrosine molecule and a leucine molecule existing at equal occupancies in both of the SGPB molecules in the asymmetric unit synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information upon the formation of the tetrahedral intermediate, residues Glu192A to Gly193 of SGPB move towards the alpha-carboxylate O of residue P1 of the bound species, and adjustments in the side-chain conformational angles of His57 and Ser195 of SGPB favor the progression of the catalytic mechanism of SGPB synthetic construct ?
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?

Synonyms

Synonyms Comment Organism
SGPB
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synthetic construct