Biochemical and Biophysical Research Communications

1962

DOI: 10.1016/0006-291x(62)90239-5

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Malonyl CoA — A new intermediate in the formation of mevalonic acid

Jonathan D. Brodie¹,

Gertrude W. Wasson²,

John W. Porter³

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1963

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Cited by 9 publications

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“…The pathway ofmevalonate biosynthesis in rat liver has now been fairly well established. The existence and subcellular localization of the enzymes between acetyl-CoA and mevalonate have been determined (White & Rudney, 1970) and the minimal physiological significance of the 'malonyl-CoA' pathway (Brodie et al, 1962(Brodie et al, , 1963 in this tissue has been demonstrated (Fimognari & Rodwell, 1970;Higgins & Kekwick, 1973).…”

mentioning

confidence: 99%

Some properties and a suggested reclassification of mevaldate reductase

¹

,

²

,

³

1974

Biochemical Journal

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Mevaldate reductase was purified 70-fold from rat liver. The partly purified enzyme had a molecular weight of 27000-30000, reduced certain aromatic aldehydes and was inhibited by barbiturates. These properties are similar to those of other animal tissue aldehyde reductases (EC 1.1.1.2) and it is suggested that mevaldate reductase be reclassified as one of this group.

“…The pathway ofmevalonate biosynthesis in rat liver has now been fairly well established. The existence and subcellular localization of the enzymes between acetyl-CoA and mevalonate have been determined (White & Rudney, 1970) and the minimal physiological significance of the 'malonyl-CoA' pathway (Brodie et al, 1962(Brodie et al, , 1963 in this tissue has been demonstrated (Fimognari & Rodwell, 1970;Higgins & Kekwick, 1973).…”

mentioning

confidence: 99%

Some properties and a suggested reclassification of mevaldate reductase

¹

,

²

,

³

1974

Biochemical Journal

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Mevaldate reductase was purified 70-fold from rat liver. The partly purified enzyme had a molecular weight of 27000-30000, reduced certain aromatic aldehydes and was inhibited by barbiturates. These properties are similar to those of other animal tissue aldehyde reductases (EC 1.1.1.2) and it is suggested that mevaldate reductase be reclassified as one of this group.

Biosynthesis of Rubber

¹

,

²

1967

Advances in Enzymology - And Related Areas of Molecular Biology

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The formation of malonyl-enzyme and its conversion to fatty acids and β-hydroxy, β-methyl glutaryl coenzyme A

¹

,

²

,

³

1963

Biochemical and Biophysical Research Communications

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No abstract

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