This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1]. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reacti ...
This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1]. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site [3]. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.
Deacetoxycephalosporin C synthase (DAOCS) from Streptomyces clavuligerus is able to catalyse the synthesis of sporins from penicillin using 2-oxoglutarate (2OG) as a co-substrate. This reaction is potentially very useful to industry because it enables processing of penicillin to other beta-lactam ring containing compounds which may not trigger antibiotic resistance systems in prokaryotes that evolved with penicillin itself as the selective agent. As with the other members of the family of 2OG utilising enzymes, DAOCS shows a beta barrel catalytic core and has its iron centre ligated to two histidines and an aspartate residue at the active site. It also displays roughly the same catalytic cycle, albeit for a specific reaction, as seen for the other members of the family, such as anthocyanidin synthase.
