This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and the other dehydrogenated.
Nomenclature
The systematic name of this enzyme class is penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding). Other names in common use include DAOCS, penicillin N expandase, and DAOC synthase.
Isopenicillin N synthase (IPNS) is a non-heme iron protein belonging to the 2-oxoglutarate (2OG)-dependent dioxygenases oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV).
In enzymology, a 2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) is an enzyme that catalyzes the chemical reaction
In enzymology, a 6β-hydroxyhyoscyamine epoxidase (EC 1.14.11.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a deacetoxycephalosporin-C hydroxylase (EC 1.14.11.26) is an enzyme that catalyzes the chemical reaction
In enzymology, a desacetoxyvindoline 4-hydroxylase (EC 1.14.11.20) is an enzyme that catalyzes the chemical reaction
In enzymology, a flavanone 3-dioxygenase (EC 1.14.11.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a flavone synthase (EC 1.14.11.22) is an enzyme that catalyzes the chemical reaction
In enzymology, a flavonol synthase is an enzyme that catalyzes the following chemical reaction :
In enzymology, a gibberellin-44 dioxygenase (EC 1.14.11.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a leucocyanidin oxygenase (EC 1.14.11.19) is an enzyme that catalyzes the chemical reaction
In enzymology, a procollagen-proline 3-dioxygenase (EC 1.14.11.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a proline 3-hydroxylase (EC 1.14.11.28) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyrimidine-deoxynucleoside 2'-dioxygenase (EC 1.14.11.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a trimethyllysine dioxygenase (TMLH; EC 1.14.11.8) is an enzyme that catalyzes the chemical reaction
In enzymology, an isopenicillin N epimerase is an enzyme that catalyzes the chemical reaction
Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) (EC 1.14.11.34, ethylene-forming enzyme, EFE) is an enzyme with systematic name L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming). This enzyme catalyses the following chemical reaction
Pentalenolactone F synthase (EC 1.14.11.36, PEND (gene), PNTD (gene), PTLD (gene)) is an enzyme with systematic name pentalenolactone-D,2-oxoglutarate:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction
Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. Functionally, the αKG-dependent hydroxylases are comparable to cytochrome P450 enzymes. Both use O2 and reducing equivalents as cosubstrates and both generate water.
Lee HJ, Lloyd MD, Harlos K, Clifton IJ, Baldwin JE, Schofield CJ (2001). "Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)". J. Mol. Biol. 308 (5): 937–48. doi:10.1006/jmbi.2001.4649. PMID11352583.
Yeh WK, Ghag SK, Queener SW (1992). "Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C Function, evolution, refolding, and enzyme engineering". Ann. N.Y. Acad. Sci. 672: 396–408. doi:10.1111/j.1749-6632.1992.tb32705.x.
Dotzlaf JE, Yeh WK (1989). "Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus". J. Biol. Chem. 264 (17): 10219–27. PMID2656705.
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