Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA

Kay Tanaka; John J. O'Shea; Gaetano Finocchiaro; Yasuyuki Ikeda; D. John Aberhart; Pallab K. Ghoshal

doi:10.1016/0167-4838(86)90059-2

Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA

Kay Tanaka, John J. O'Shea, Gaetano Finocchiaro, Yasuyuki Ikeda, D. John Aberhart, Pallab K. Ghoshal

Fondazione IRCCS Istituto Neurologico "C. Besta"

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

Abstract

Dehydrogenation of (2S)-[3-¹³C]isobutyryl-CoA was carried out in vitro using 2-methyl-branched-chain acyl-CoA dehydrogenase purified from rat liver mitochondria. The product was subsequently hydrated by the addition of bovine crotonase. The resulting 3-hydroxyisobutyric acid was predominantly enriched with ¹³C at the β-hydroxy position as determined as a methyl ester using electron ionization-gas chromatography-mass spectroscopy. This finding indicates that isobutyryl-CoA is dehydrogenated stereospecifically at the (pro-2S)-methyl and α-methine groups to form methacrylyl-CoA, which is later hydrated with the addition of hydrogen on the same side of the molecule from which it was subtracted to produce 3-hydroxyisobutyryl-CoA.

Original language	English
Pages (from-to)	308-311
Number of pages	4
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	873
Issue number	2
DOIs	https://doi.org/10.1016/0167-4838(86)90059-2
Publication status	Published - Sep 26 1986

Keywords

2-methyl-branched-chain acyl-CoA
Acyl-CoA dehydrogenase
Substrate stereochemistry

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology
Structural Biology

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10.1016/0167-4838(86)90059-2

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Tanaka, K., O'Shea, J. J., Finocchiaro, G., Ikeda, Y., Aberhart, D. J., & Ghoshal, P. K. (1986). Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 873(2), 308-311. https://doi.org/10.1016/0167-4838(86)90059-2

Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase : elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA. / Tanaka, Kay; O'Shea, John J.; Finocchiaro, Gaetano; Ikeda, Yasuyuki; Aberhart, D. John; Ghoshal, Pallab K.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 873, No. 2, 26.09.1986, p. 308-311.

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

Tanaka, K, O'Shea, JJ, Finocchiaro, G, Ikeda, Y, Aberhart, DJ & Ghoshal, PK 1986, 'Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA', Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, vol. 873, no. 2, pp. 308-311. https://doi.org/10.1016/0167-4838(86)90059-2

Tanaka K, O'Shea JJ, Finocchiaro G, Ikeda Y, Aberhart DJ, Ghoshal PK. Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1986 Sep 26;873(2):308-311. https://doi.org/10.1016/0167-4838(86)90059-2

Tanaka, Kay ; O'Shea, John J. ; Finocchiaro, Gaetano ; Ikeda, Yasuyuki ; Aberhart, D. John ; Ghoshal, Pallab K. / Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase : elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1986 ; Vol. 873, No. 2. pp. 308-311.

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abstract = "Dehydrogenation of (2S)-[3-13C]isobutyryl-CoA was carried out in vitro using 2-methyl-branched-chain acyl-CoA dehydrogenase purified from rat liver mitochondria. The product was subsequently hydrated by the addition of bovine crotonase. The resulting 3-hydroxyisobutyric acid was predominantly enriched with 13C at the β-hydroxy position as determined as a methyl ester using electron ionization-gas chromatography-mass spectroscopy. This finding indicates that isobutyryl-CoA is dehydrogenated stereospecifically at the (pro-2S)-methyl and α-methine groups to form methacrylyl-CoA, which is later hydrated with the addition of hydrogen on the same side of the molecule from which it was subtracted to produce 3-hydroxyisobutyryl-CoA.",

keywords = "2-methyl-branched-chain acyl-CoA, Acyl-CoA dehydrogenase, Substrate stereochemistry",

author = "Kay Tanaka and O'Shea, {John J.} and Gaetano Finocchiaro and Yasuyuki Ikeda and Aberhart, {D. John} and Ghoshal, {Pallab K.}",

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AU - Tanaka, Kay

AU - O'Shea, John J.

AU - Finocchiaro, Gaetano

AU - Ikeda, Yasuyuki

AU - Aberhart, D. John

AU - Ghoshal, Pallab K.

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AB - Dehydrogenation of (2S)-[3-13C]isobutyryl-CoA was carried out in vitro using 2-methyl-branched-chain acyl-CoA dehydrogenase purified from rat liver mitochondria. The product was subsequently hydrated by the addition of bovine crotonase. The resulting 3-hydroxyisobutyric acid was predominantly enriched with 13C at the β-hydroxy position as determined as a methyl ester using electron ionization-gas chromatography-mass spectroscopy. This finding indicates that isobutyryl-CoA is dehydrogenated stereospecifically at the (pro-2S)-methyl and α-methine groups to form methacrylyl-CoA, which is later hydrated with the addition of hydrogen on the same side of the molecule from which it was subtracted to produce 3-hydroxyisobutyryl-CoA.

KW - 2-methyl-branched-chain acyl-CoA

KW - Acyl-CoA dehydrogenase

KW - Substrate stereochemistry

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Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA

Abstract

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