Gibberellins are essential plant hormones that regulate growth and development. Besides plants, phytopathogenic fungi and plant‐associated bacteria also produce gibberellins. The recently elucidated bacterial pathway uses four soluble cytochromes P450 (CYPs) for gibberellin biosynthesis. While the sequence of the reactions is exactly the same as the plant pathway, rather than two 2ODDs for the last two steps bacteria use two CYPs instead. We have successfully expressed the CYP117 responsible for the oxidation of ent‐kaurene to ent‐kaurenoic acid and with 18O2 labelling experiments could identify the sequence of catalysed reactions in this multistep transformation. The next biosynthetic step is the coupled formation of an aldehyde with ring contraction, here using UV/VIS‐spectroscopy we have determined the binding affinities of the relevant CYP114 for its substrate, ent‐kaurenoic acid, as well as close structural analogues. Notably the ring contraction reaction relies on a specific ferredoxin; other ferredoxins only enable production of the intermediate ent‐7a‐hydroxykaurenoic acid. Subsequently, CYP112 catalyses a series of reactions that lead to coupled demethylation‐lactone ring formation, transforming GA12 into GA9. Again we have used UV/VIS‐spectroscopy to determine the binding affinities of CYP112 for the substrate GA9 as well as both intermediates (GA15 and GA24), and multiple structural analogues. In addition, we also performed 18O2 labeling experiments with CYP112 that establish the sequence of catalysed reactions in this multistep transformation, and show that the carbon lost in the demethylation reaction leaves as CO2.