Stereospecificity of hydrogen transfer from NADPH by steroid Δ4-5α- and Δ4-5β-reductase

Yusuf J. Abul-Hajj

doi:10.1016/0039-128X(72)90081-5

Stereospecificity of hydrogen transfer from NADPH by steroid Δ⁴-5α- and Δ⁴-5β-reductase

Yusuf J. Abul-Hajj

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

36 Scopus citations

Abstract

The saturation of the C-4,5 double bond of Δ⁴-3-ketosteroids catalyzed by Δ⁴-3-ketosteroid-5β-reductase has been shown to involve a hydride ion transfer from the A-position of NADPH to the 5β-position of the steroid while the reaction catalyzed by Δ⁴-3-ketosteroid-5α-reductase involves a hydride transfer from the B-position of NADPH to the 5α-position of the steroid. Thus, this study shows that Δ⁴-5β-reductase has A-stereospecificity while Δ⁴-5α-reductase has B-stereospecificity.

Original language	English (US)
Pages (from-to)	215-222
Number of pages	8
Journal	Steroids
Volume	20
Issue number	3
DOIs	https://doi.org/10.1016/0039-128X(72)90081-5
State	Published - Sep 1972
Externally published	Yes

Publisher link

10.1016/0039-128X(72)90081-5

Find It

Find It at U of M Libraries

Cite this

@article{5c09b5eb41794ef4978362879a25f15e,

title = "Stereospecificity of hydrogen transfer from NADPH by steroid Δ4-5α- and Δ4-5β-reductase",

abstract = "The saturation of the C-4,5 double bond of Δ4-3-ketosteroids catalyzed by Δ4-3-ketosteroid-5β-reductase has been shown to involve a hydride ion transfer from the A-position of NADPH to the 5β-position of the steroid while the reaction catalyzed by Δ4-3-ketosteroid-5α-reductase involves a hydride transfer from the B-position of NADPH to the 5α-position of the steroid. Thus, this study shows that Δ4-5β-reductase has A-stereospecificity while Δ4-5α-reductase has B-stereospecificity.",

author = "Abul-Hajj, \{Yusuf J.\}",

year = "1972",

month = sep,

doi = "10.1016/0039-128X(72)90081-5",

language = "English (US)",

volume = "20",

pages = "215--222",

journal = "Steroids",

issn = "0039-128X",

publisher = "Elsevier Inc.",

number = "3",

}

TY - JOUR

T1 - Stereospecificity of hydrogen transfer from NADPH by steroid Δ4-5α- and Δ4-5β-reductase

AU - Abul-Hajj, Yusuf J.

PY - 1972/9

Y1 - 1972/9

N2 - The saturation of the C-4,5 double bond of Δ4-3-ketosteroids catalyzed by Δ4-3-ketosteroid-5β-reductase has been shown to involve a hydride ion transfer from the A-position of NADPH to the 5β-position of the steroid while the reaction catalyzed by Δ4-3-ketosteroid-5α-reductase involves a hydride transfer from the B-position of NADPH to the 5α-position of the steroid. Thus, this study shows that Δ4-5β-reductase has A-stereospecificity while Δ4-5α-reductase has B-stereospecificity.

AB - The saturation of the C-4,5 double bond of Δ4-3-ketosteroids catalyzed by Δ4-3-ketosteroid-5β-reductase has been shown to involve a hydride ion transfer from the A-position of NADPH to the 5β-position of the steroid while the reaction catalyzed by Δ4-3-ketosteroid-5α-reductase involves a hydride transfer from the B-position of NADPH to the 5α-position of the steroid. Thus, this study shows that Δ4-5β-reductase has A-stereospecificity while Δ4-5α-reductase has B-stereospecificity.

UR - https://www.scopus.com/pages/publications/0015402161

UR - https://www.scopus.com/pages/publications/0015402161#tab=citedBy

U2 - 10.1016/0039-128X(72)90081-5

DO - 10.1016/0039-128X(72)90081-5

M3 - Article

C2 - 4403723

AN - SCOPUS:0015402161

SN - 0039-128X

VL - 20

SP - 215

EP - 222

JO - Steroids

JF - Steroids

IS - 3

ER -

Stereospecificity of hydrogen transfer from NADPH by steroid Δ⁴-5α- and Δ⁴-5β-reductase

Abstract

Publisher link

Find It

Other files and links

Fingerprint

Cite this