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Literature summary for 1.14.15.8 extracted from

  • Ruijssenaars, H.J.; Sperling, E.M.; Wiegerinck, P.H.; Brands, F.T.; Wery, J.; de Bont, J.A.
    Testosterone 15beta-hydroxylation by solvent tolerant Pseudomonas putida S12 (2007), J. Biotechnol., 131, 205-208.
    View publication on PubMed

Application

Application Comment Organism
synthesis a steroid 15beta-hydroxylating whole-cell solvent tolerant biocatalyst is constructed by expressing the Bacillus megaterium steroid hydroxylase CYP106A2 in the solvent tolerant Pseudomonas putida S12. Testosterone hydroxylation is improved by a factor 16 by co-expressing Fer, a putative Fe-S protein from Bacillus subtilis. The specificity for 15beta-hydroxylation is improved by mutating threonine residue 248 of CYP106A2 into valine. These insights provide the basis for an optimized whole-cell steroid-hydroxylating biocatalyst that can be applied with an organic solvent phase Priestia megaterium

Cloned(Commentary)

Cloned (Comment) Organism
a steroid 15beta-hydroxylating whole-cell solvent tolerant biocatalyst is constructed by expressing the Bacillus megaterium steroid hydroxylase CYP106A2 in the solvent tolerant Pseudomonas putida S12 Priestia megaterium

Protein Variants

Protein Variants Comment Organism
T248V specificity for 15beta-hydroxylation is improved Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
testosterone + reduced acceptor + O2 the major product is identified as 15beta-hydroxytestosterone. 6beta-Hydroxytestosterone and androst-4-ene-3,17-dione are present as minor products Priestia megaterium 15beta-hydroxytestosterone + oxidized acceptor + H2O
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