1987
DOI: 10.1016/0020-711x(87)90185-6
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Purification and properties of aldehyde dehydrogenase from Aspergillus nidulans

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Cited by 10 publications
(6 citation statements)
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“…We presume that this inducer is acetaldehyde formed for instance by L-threonine turnover (38) or by constitutive pyruvate decarboxylase activity (39). Acetaldehyde is the main substrate for A. nidulans ALDH in vitro (17). A similar situation occurs in case of the A. nidulans purine utilization pathway.…”
Section: Structural Mutations In Alda Give Rise To Induction Of the Amentioning
confidence: 90%
See 1 more Smart Citation
“…We presume that this inducer is acetaldehyde formed for instance by L-threonine turnover (38) or by constitutive pyruvate decarboxylase activity (39). Acetaldehyde is the main substrate for A. nidulans ALDH in vitro (17). A similar situation occurs in case of the A. nidulans purine utilization pathway.…”
Section: Structural Mutations In Alda Give Rise To Induction Of the Amentioning
confidence: 90%
“…it is unable to reduce acetate (16). This irreversible conversion drives ethanol catabolism (17). Moreover, acetaldehyde is the first intermediate common to ethanol, L-threonine, and ethylamine utilization, all processes provoking induction of the alc gene system (1,3,5,18,19).…”
mentioning
confidence: 99%
“…It is generally recognized that enzyme activities depending on essential thiol groups are extremely susceptible to aldehyde inactivation. A. nidulans ALDH itself is inhibited in itro at concentrations above 350 µM [23], which could match the intracellular concentration at which acetaldehyde starts to affect cellular functioning. Note here that formaldehyde, the smallest aldehyde, proved to be too toxic at all concentrations tested.…”
Section: Aldehydes Induce Alc Gene Transcription At Low External Concmentioning
confidence: 99%
“…-Threonine can also serve as a sole source of both carbon and nitrogen for A. nidulans. This amino acid is converted into acetaldehyde and glycine by threonine aldolase (EC 4.1.2.5) [23], this conversion being common in mammals and in yeasts. In baker's yeast (Saccharomyces cereisiae), this enzyme is essential for the biosynthesis of glycine when cells are grown on -glucose [24].…”
Section: Introductionmentioning
confidence: 99%
“…Alcohol dehydrogenase 1 (ADH1) and aldehyde dehydrogenase (AldDH) activities were determined as described (10)(11)(12), except that cell-free protein extracts were made by using lyophilized cells. Protein concentrations were determined by the Bradford procedure (13).…”
mentioning
confidence: 99%