Mechanism of 17[alpha]-hydroxylase/17,20-lyase--an initial geometric perspective for the lyase of the C(17)-C(20) bond of C[sub]21 steroids

Sabbir Ahmed; Caroline P. Owen

doi:10.1016/S0960-894X(98)00154-1

Mechanism of 17[alpha]-hydroxylase/17,20-lyase--an initial geometric perspective for the lyase of the C(17)-C(20) bond of C[sub]21 steroids

Sabbir Ahmed
, Caroline P. Owen

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	1023-1028
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	8
Issue number	9
DOIs	https://doi.org/10.1016/S0960-894X(98)00154-1
Publication status	Published - 5 May 1998
Externally published	Yes

Keywords

inhibitors
aromatase
Chemistry

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10.1016/S0960-894X(98)00154-1

http://dx.doi.org/10.1016/S0960-894X(98)00154-1

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title = "Mechanism of 17[alpha]-hydroxylase/17,20-lyase--an initial geometric perspective for the lyase of the C(17)-C(20) bond of C[sub]21 steroids",

abstract = "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.",

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AU - Ahmed, Sabbir

AU - Owen, Caroline P.

PY - 1998/5/5

Y1 - 1998/5/5

N2 - 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.

AB - 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.

KW - inhibitors

KW - aromatase

KW - Chemistry

UR - http://www.ncbi.nlm.nih.gov/pubmed/9871701

U2 - 10.1016/S0960-894X(98)00154-1

DO - 10.1016/S0960-894X(98)00154-1

M3 - Article

C2 - 9871701

SN - 0960-894X

VL - 8

SP - 1023

EP - 1028

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 9

ER -

Mechanism of 17[alpha]-hydroxylase/17,20-lyase--an initial geometric perspective for the lyase of the C(17)-C(20) bond of C[sub]21 steroids

Abstract

Keywords

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