1981
DOI: 10.1016/0031-9422(81)83007-5
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The effect of some phenolic compounds on the activity of 6-phosphogluconate dehydrogenase from tobacco tissue cultures

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1982
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Cited by 16 publications
(3 citation statements)
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“…In contrast, 6PG levels did not significantly differ among the three conditions, indicating that the activity of 6PG dehydrogenase, which catalyzes the rate-limiting NADPH-producing step in the PPP, was attenuated by an unknown factor in the hydrolysates. This conclusion is supported by a previous observation that lignin derivatives of coumaric acid and ferulic acid inhibit 6PG dehydrogenase in plant cells (Al-Quadan et al, 1981), although similar inhibition has not been reported in E. coli. Intracellular levels of E4P, a precursor of aromatic acid biosynthesis via the shikimate pathway, were markedly reduced in cells cultured with the lignocellulosic hydrolysates, particularly that of sorghum bagasse.…”
Section: Metabolomic Analysis Of E Coli Cells During Phla Metabolismsupporting
confidence: 72%
“…In contrast, 6PG levels did not significantly differ among the three conditions, indicating that the activity of 6PG dehydrogenase, which catalyzes the rate-limiting NADPH-producing step in the PPP, was attenuated by an unknown factor in the hydrolysates. This conclusion is supported by a previous observation that lignin derivatives of coumaric acid and ferulic acid inhibit 6PG dehydrogenase in plant cells (Al-Quadan et al, 1981), although similar inhibition has not been reported in E. coli. Intracellular levels of E4P, a precursor of aromatic acid biosynthesis via the shikimate pathway, were markedly reduced in cells cultured with the lignocellulosic hydrolysates, particularly that of sorghum bagasse.…”
Section: Metabolomic Analysis Of E Coli Cells During Phla Metabolismsupporting
confidence: 72%
“…Polypeptides of 55 kD were present at dramatically reduced levels in leaf extracts from the 6-PGD double-null homozygote. Thus, the subunit molecular mass of cytosolic 6-PGD from maize is similar to that of enzymes purified from other plants (1,8,10), fungi, animals, and bacteria (7). The analysis also demonstrated minor differences in the amounts of a few other proteins purified from leaves of the two genotypes.…”
Section: Discussionmentioning
confidence: 66%
“…Both forms of G6PDH are inactivated by light via a redox-regulated reaction [2]. Phenylpropanoid pathway intermediates have been shown to inhibit both tobacco 6PGDH isoenzymes [ 1 ], although the physiological significance of this is not clear. It is not known whether the increased activities of the pentose phosphate pathway enzymes measured in crude extracts from elicited cells reflect transcriptional, post-transcriptional or metabolic regulation.…”
Section: Introductionmentioning
confidence: 99%