Literature summary 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.

Application

EC Number	Application	Comment	Organism
1.14.15.8	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)

EC Number	Cloned (Comment)	Organism
1.14.15.8	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

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.15.8	Priestia megaterium	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.15.8	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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Release 2023.1 (January 2023)