TY - JOUR
T1 - Crystal structure and site-directed mutagenesis of 3-ketosteroid δ1-dehydrogenase from rhodococcus erythropolis SQ1 explain its catalytic mechanism
AU - Rohman, Ali
AU - Van Oosterwijk, Niels
AU - Thunnissen, Andy Mark W.H.
AU - Dijkstra, Bauke W.
PY - 2013/12/6
Y1 - 2013/12/6
N2 - Background: 3-Ketosteroid δ1-dehydrogenases catalyze the 1,2-desaturation of 3-ketosteroids. Results: First structures of the enzyme from Rhodococcus erythropolis SQ1, combined with site-directed mutagenesis, clarify its catalytic mechanism. Conclusion: Tyr487 and Gly491 promote keto-enol tautomerization, whereas Tyr318/Tyr119 and FAD abstract a proton and hydride ion, respectively. Significance: This study is an important step toward tailoring the enzyme for steroid biotransformation applications.
AB - Background: 3-Ketosteroid δ1-dehydrogenases catalyze the 1,2-desaturation of 3-ketosteroids. Results: First structures of the enzyme from Rhodococcus erythropolis SQ1, combined with site-directed mutagenesis, clarify its catalytic mechanism. Conclusion: Tyr487 and Gly491 promote keto-enol tautomerization, whereas Tyr318/Tyr119 and FAD abstract a proton and hydride ion, respectively. Significance: This study is an important step toward tailoring the enzyme for steroid biotransformation applications.
UR - http://www.scopus.com/inward/record.url?scp=84890281500&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.522771
DO - 10.1074/jbc.M113.522771
M3 - Article
C2 - 24165124
AN - SCOPUS:84890281500
SN - 0021-9258
VL - 288
SP - 35559
EP - 35568
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 49
ER -