EC Number |
General Information |
Reference |
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3.5.1.93 | more |
three-dimensional structure model of wild-type enzyme, overview |
720077 |
3.5.1.93 | more |
the protein structure of Pseudomonas SE83 CCA is obtained through the computational modeling with X-ray crystal structure of Pseudomonas N176 CCA (PDB accession code 4HST) as the template, three-dimensional structure, homology modeling, overview. The key residue of the enzyme, 1Ser of beta-subunit, is located in the active-site cavity, which is on the opposite side to the C-terminal of beta-subunit |
733139 |
3.5.1.93 | more |
a deep cavity constitutes the active site, structure overview. The nucleophilic catalytic serine residue, Ser1beta, is situated at the base of the active site cavity, ligand covalently binds to the catalytic serine residue forming a tetrahedral adduct and mimickingc the transition state of the enzyme for both the maturation step and the catalysis of the substrates |
733289 |
3.5.1.93 | evolution |
phylogenetic analysis and active site evolution concerning cephalosporin C binding, overview |
733836 |
3.5.1.93 | more |
substrate binding, molecular modeling study, overview |
733836 |
3.5.1.93 | evolution |
the enzyme is a member of the N-terminal nucleophile (Ntn) hydrolase superfamily, in which the precursor gene is translated into a single polypeptide chain and then folded into a self-activating pre-protein activated by intramolecular double cleavages |
734344 |
3.5.1.93 | more |
structure-activity modelling using wild-type and mutant enzymes, active site structures, overview |
755869 |
3.5.1.93 | physiological function |
cephalosporin C acylase is the key enzyme catalyst for the hydrolysis of cephalosporin C (CPC), which directly produces the important cephalosporin antibiotic 7-aminocephalosporanic acid (7-ACA). 7-ACA is an important cephalosporin nucleus for the synthesis of many widely used beta-lactam antibiotics |
756519 |
3.5.1.93 | evolution |
the antibiotic acylases belong to the N-terminal nucleophile hydrolase superfamily |
758270 |
3.5.1.93 | metabolism |
antibiotic acylases cephalosporin acylase and penicillin G acylase (EC 3.5.1.11) catalyze the deacylation of beta-lactam antibiotics, while aculeacin A acylase (EC 3.5.1.70) is known to be an alternative acylase class catalyzing the deacylation of echinocandin or cyclic lipopeptide antibiotic compounds |
758270 |