Mechanism of 17 alpha-hydroxylase/17,20-lyase--an initial geometric perspective for the lyase of the C(17)-C(20) bond of C21 steroids.
Using the novel 'substrate-heme complex' approach, the mechanism of 17 alpha-Hydroxylase/17,20-Lyase (P-450(17) alpha), in particular the lyase of the C(17)-C(20) bond, is considered from a geometric perspective. The results of the study appear to suggest that the final oxidative step in the lyase of the C(17)-C(20) bond involves the use of a ferroxy attacking species as opposed to peroxy or a mixture of ferroxy and peroxy, an observation which is consistent with results previously obtained with Aromatase.
Ahmed
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S
School of Applied Chemistry, Kingston University, Kingston upon Thames, Surrey, UK. CH_S534@KINGSTON.AC.UK
Owen
C P
CP
D006907:17-alpha-Hydroxypregnenolone / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism; D001141:Aromatase / Q000378:metabolism; D001665:Binding Sites; D006418:Heme; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D010545:Peroxides; D013254:Steroid 17-alpha-Hydroxylase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D010545:Peroxides; D006907:17-alpha-Hydroxypregnenolone; D006418:Heme; D001141:Aromatase; D013254:Steroid 17-alpha-Hydroxylase