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Corticosteroid Biosynthesis Revisited: Substrate Specificity of Steroid 21‐Hydroxylase
Author(s) -
Loke Steffen,
Stoll Anna,
Joseph Jan Felix,
Machalz David,
de la Torre Xavier,
Botrè Francesco,
Wolber Gerhard,
Bureik Matthias,
Parr Maria
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.03869
Subject(s) - pregnenolone , steroid , chemistry , biotransformation , cytochrome p450 , steroid hormone , enzyme , biochemistry , protein data bank (rcsb pdb) , steroid biosynthesis , hydroxylation , biosynthesis , hormone
METHODS • biotransformation experiments were performed with a fission yeast expressing human CYP21A2 (CAD75) in a whole-cell biotransformation assay • progesterone, pregnenolone and their corresponding 17-hydroxy analogs were used as substrates • analysis by GC-MS as TMS-derivatives • molecular docking were performed using GOLD software (CYP21A2 co-crystallized with progesterone) RESULTS • 21-hydroxylation of (17OH-)progesterone successful • 21-hydroxylation of (17OH-)pregnenolone not prosperous • essential interaction between 3-oxo and Arg234 of CYP21 shown by molecular docking experiments