Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia

Alex Chu; Albena Dinkova; Laurence B. Davin; Diana L. Bedgar; Norman G. Lewis

Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia

Alex Chu
, Albena Dinkova
, Laurence B. Davin
, Diana L. Bedgar
, Norman G. Lewis

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

Abstract

Pinoresinol/lariciresinol reductase catalyzes the first known example of a highly unusual benzylic ether reduction in plants; its mechanism of hydride transfer is described. The enzyme was found in Forsythia intermedia and catalyzes the presumed regulatory branch-points in the pathway leading to benzylaryltetrahydrofuran, dibenzylbutane, dibenzylbutyrolactone, and aryltetrahydronaphthalene lignans. Using [7,7′-²H₂]-pinoresinol and [7,7′-²H₃]lariciresinol as substrates, the hydride transfers of the highly unusual reductase were demonstrated to be completely stereospecific (>99%). The incoming hydrides were found to take up the pro-R position at C-7′ (and/or C-7) in lariciresinol and secoisolariciresinol, thereby eliminating the possibility of random hydride delivery to a planar quinone methide intermediate. As might be expected, the mode of hydride abstraction from NADPH was also stereospecific: using [4A-³H] and [4S-³H]NADPH, it was found that only the 4 pro-R hydrogen was abstracted for enzymatic hydride transfer.

Original language	English
Pages (from-to)	27026-27033
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	268
Issue number	36
Publication status	Published - 25 Dec 1993

ASJC Scopus subject areas

Biochemistry

Cite this

@article{d0a36c26e3f94cf4a11a0730b3c4574b,

title = "Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia",

abstract = "Pinoresinol/lariciresinol reductase catalyzes the first known example of a highly unusual benzylic ether reduction in plants; its mechanism of hydride transfer is described. The enzyme was found in Forsythia intermedia and catalyzes the presumed regulatory branch-points in the pathway leading to benzylaryltetrahydrofuran, dibenzylbutane, dibenzylbutyrolactone, and aryltetrahydronaphthalene lignans. Using [7,7′-2H2]-pinoresinol and [7,7′-2H3]lariciresinol as substrates, the hydride transfers of the highly unusual reductase were demonstrated to be completely stereospecific (>99\%). The incoming hydrides were found to take up the pro-R position at C-7′ (and/or C-7) in lariciresinol and secoisolariciresinol, thereby eliminating the possibility of random hydride delivery to a planar quinone methide intermediate. As might be expected, the mode of hydride abstraction from NADPH was also stereospecific: using [4A-3H] and [4S-3H]NADPH, it was found that only the 4 pro-R hydrogen was abstracted for enzymatic hydride transfer.",

author = "Alex Chu and Albena Dinkova and Davin, \{Laurence B.\} and Bedgar, \{Diana L.\} and Lewis, \{Norman G.\}",

year = "1993",

month = dec,

day = "25",

language = "English",

volume = "268",

pages = "27026--27033",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "36",

}

TY - JOUR

T1 - Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia

AU - Chu, Alex

AU - Dinkova, Albena

AU - Davin, Laurence B.

AU - Bedgar, Diana L.

AU - Lewis, Norman G.

PY - 1993/12/25

Y1 - 1993/12/25

N2 - Pinoresinol/lariciresinol reductase catalyzes the first known example of a highly unusual benzylic ether reduction in plants; its mechanism of hydride transfer is described. The enzyme was found in Forsythia intermedia and catalyzes the presumed regulatory branch-points in the pathway leading to benzylaryltetrahydrofuran, dibenzylbutane, dibenzylbutyrolactone, and aryltetrahydronaphthalene lignans. Using [7,7′-2H2]-pinoresinol and [7,7′-2H3]lariciresinol as substrates, the hydride transfers of the highly unusual reductase were demonstrated to be completely stereospecific (>99%). The incoming hydrides were found to take up the pro-R position at C-7′ (and/or C-7) in lariciresinol and secoisolariciresinol, thereby eliminating the possibility of random hydride delivery to a planar quinone methide intermediate. As might be expected, the mode of hydride abstraction from NADPH was also stereospecific: using [4A-3H] and [4S-3H]NADPH, it was found that only the 4 pro-R hydrogen was abstracted for enzymatic hydride transfer.

AB - Pinoresinol/lariciresinol reductase catalyzes the first known example of a highly unusual benzylic ether reduction in plants; its mechanism of hydride transfer is described. The enzyme was found in Forsythia intermedia and catalyzes the presumed regulatory branch-points in the pathway leading to benzylaryltetrahydrofuran, dibenzylbutane, dibenzylbutyrolactone, and aryltetrahydronaphthalene lignans. Using [7,7′-2H2]-pinoresinol and [7,7′-2H3]lariciresinol as substrates, the hydride transfers of the highly unusual reductase were demonstrated to be completely stereospecific (>99%). The incoming hydrides were found to take up the pro-R position at C-7′ (and/or C-7) in lariciresinol and secoisolariciresinol, thereby eliminating the possibility of random hydride delivery to a planar quinone methide intermediate. As might be expected, the mode of hydride abstraction from NADPH was also stereospecific: using [4A-3H] and [4S-3H]NADPH, it was found that only the 4 pro-R hydrogen was abstracted for enzymatic hydride transfer.

UR - https://www.scopus.com/pages/publications/0027756968

M3 - Article

C2 - 8262939

AN - SCOPUS:0027756968

SN - 0021-9258

VL - 268

SP - 27026

EP - 27033

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 36

ER -

Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia

Abstract

ASJC Scopus subject areas

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