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Literature summary for 2.3.1.18 extracted from

  • Ballano, G.; Zanuy, D.; Jimenez, A.I.; Cativiela, C.; Nussinov, R.; Aleman, C.
    Structural analysis of a beta-helical protein motif stabilized by targeted replacements with conformationally constrained amino acids (2008), J. Phys. Chem. B, 112, 13101-13115.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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Escherichia coli

Protein Variants

Protein Variants Comment Organism
G149Ac3c glycine is substituted by the constrained amino acids 1-aminocyclopropane-1-carboxylic acid, from protein chain A peptide from residues 131-165 are synthetical produced and investigated, the mutated peptide has a reduce conformational flexibility Escherichia coli
G149Ac5c glycine is substituted by the constrained amino acids 1-aminocyclopentane-1-carboxylic acid, from protein chain A peptide from residues 131-165 are synthetical produced and investigated, the mutated peptide has a reduce conformational flexibility Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P07464 from chain A residues 131-165 are prepared as synthetical peptide and investigated
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Synonyms

Synonyms Comment Organism
galactoside acetyltransferase
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Escherichia coli