Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat liver

Mahadevan, S.; Murthy, S. K.; Ganguly, J.

doi:10.1042/bj0850326

Cited by 52 publications

(20 citation statements)

References 16 publications

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“…Studies from several groups provided evidence that the aldehyde form of vitamin A was oxidized irreversibly to vitamin A acid, and that this reaction was catalyzed by aldehyde dehydrogenases (ALDHs) in calf and rat liver (Dmitrovskii 1961; Futterman 1962; Elder and Topper 1962; Mahadevan et al 1962; Dunagin et al 1964; Lakshmanan et al 1964) (Figure 1, step 2). Thus, it was concluded that together with alcohol dehydrogenase, the aldehyde-oxidizing enzymes provided a pathway from the vitamin A alcohol to the acid (Dmitrovsky, 1961; Futterman, 1962; Bamji et al 1962; Mahadevan et al 1962), similarly to the metabolism of ethanol to acetaldehyde and further to acetic acid.…”

Section: 2 Historymentioning

confidence: 99%

Retinoic Acid Synthesis and Degradation

Kedishvili

2016

Subcellular Biochemistry

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Retinoic acid was identified as the biologically active form of vitamin A almost 70 years ago, but the exact enzymes and control mechanisms that regulate its biosynthesis and degradation are yet to be fully defined. The currently accepted model postulates that RA is produced in two sequential oxidative steps: first, retinol is oxidized reversibly to retinaldehyde, and then retinaldehyde is oxidized irreversibly to RA, which is inactivated by conversion to hydroxylated derivatives. This chapter describes the history, development and recent advances in our understanding of the enzymatic pathways and mechanisms that control the rate of RA production and degradation. Gene knockout studies provided strong evidence that the members of the short chain dehydrogenase reductase superfamily of proteins play indispensable roles in retinoic acid biosynthesis during development. Furthermore, recent finding that two of these proteins regulate the rate of retinoic acid biosynthesis by mutually activating each other provided a novel insight into the mechanism of this regulation. Despite significant progress made since the middle of the 20th century many unanswered questions still remain, and there is much to be learned, especially about trafficking of the hydrophobic retinoid substrates between membrane bound and cytosolic enzymes and the roles of the retinoid binding proteins.

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Section: 2 Historymentioning

confidence: 99%

Retinoic Acid Synthesis and Degradation

Kedishvili

2016

Subcellular Biochemistry

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“…Sources of materials. The sources of the materials used in the present investigation have already been described Mahadevan, Murthy & Ganguly, 1962;Mahadevan et al 1963).…”

Section: Methodsmentioning

confidence: 99%

“…The procedures adopted for the extraction, paper-chromatographic separation and estimation of the different retinyl esters were as described by . The chromatographic separation of retinal from retinyl esters and retinol, and its subsequent determination, with thiobarbituric acid, were carried out as described by Mahadevan et al (1962).…”

Section: Methodsmentioning

confidence: 99%

The fate of intracardially administered retinyl esters in the rat

Mahadevan¹,

Deshmukh²,

Ganguly³

1964

Biochemical Journal

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“…The addition of various steroid hormones modifies the oxidation of retinal and propionaldehyde in a somewhat different manner, indicating differences in the enzymatic reactions of the substrates (18). A rat liver enzyme which catalyzes the oxidation and reduction of retinal to vitamin A acid and alcohol, respectively, is inhibited by p-chloromercuribenzoate, arsenite, and a number of chelating agents; inactivated enzyme is reactivated by Fe++ or when dialyzed, by FAD (19,20) . .B-8'-Apocarotenal, a homologue of vitamin A aldehyde, which is widely distributed in natural material (21), is converted into the corresponding carotenoic acid in rats, chicks, and dogs (22,23,24) and differs in this respect from vitamin A aldehyde from which an in vivo conversion into vitamin A acid could not be demonstrated (16).…”

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confidence: 97%