EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.93 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.93 | Pseudomonas sp. | A4ZVL3 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.5.1.93 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.93 | GCA | - |
Pseudomonas sp. GK16 |
3.5.1.93 | glutaryl 7-aminocephalosporanic acid acylase | - |
Pseudomonas sp. GK16 |