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Literature summary for 3.5.1.93 extracted from

  • Cho, K.J.; Kim, J.K.; Lee, J.H.; Shin, H.J.; Park, S.S.; Kim, K.H.
    Structural features of cephalosporin acylase reveal the basis of autocatalytic activation (2009), Biochem. Biophys. Res. Commun., 390, 342-348.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces the active enzyme Pseudomonas sp. GK16

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli BL21/DE3 using he pET23d plasmids harboring the cloned mature cephalosporin acylase gene from Pseudomonas sp. GK16 and the mutant genes E159M, D161N, D161L, L165N, Q168P, and L379N. The mutant proteins are overexpressed and purified Pseudomonas sp. GK16

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystals of Y202L mutants including intermediates, Y202L-I, Y202-II and Y202L-II, and Q168P and L379N are grown at 22°C using the hanging-drop vapor diffusion method. The three dimensional structures are determined at 2-2.5 A resolution. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt different loop conformations from one another. The autoproteolytic site is found to form catalytically competent conformation with a solvent water molecule, which is essentially conserved in the cephalosporin acylase mutants Pseudomonas sp. GK16

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. GK16 A4ZVL3
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Purification (Commentary)

Purification (Comment) Organism
overexpressed mutant protein Pseudomonas sp. GK16

Synonyms

Synonyms Comment Organism
cephalosporin acylase a member of the N-terminal nucleophile hydrolase family Pseudomonas sp. GK16