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Literature summary for 3.5.1.93 extracted from

  • Kim, J.K.; Yang, I.S.; Rhee, S.; Dauter, Z.; Lee, Y.S.; Park, S.S.; Kim, K.H.
    Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation (2003), Biochemistry, 42, 4084-4093.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method using ammonium sulfate as a precipitating agent, crystal structures of the recombinant selenomethionyl native and S170A mutant precursor Pseudomonas sp. GK16

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. A4ZVL3
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification activation of precursor consists of primary and secondary autoproteolytic cleavages, generating a terminal residue with both a nucleophile and a base and releasing a nine amino acid spacer peptide. Precursor activation is likely triggered by conformational constraints within the spacer peptide, probably inducing a peptide flip. Autoproteolytic site solvent molecules, which have been trapped in a hydrophobic environment by the spacer peptide, may play a role as a general base for nucleophilic attack. The activation results in building up a catalytic triad composed of Ser170/His192/Glu624. The triad is not linked to the usual hydroxyl but the free R-amino group of the N-terminal serine residue of the native enzyme. Stabilization of a transient hydroxazolidine ring during autoproteolysis would be critical during the N to O acyl shift Pseudomonas sp. GK16

Synonyms

Synonyms Comment Organism
GCA
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Pseudomonas sp. GK16
glutaryl 7-aminocephalosporanic acid acylase
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Pseudomonas sp. GK16