Acetyl Coenzyme A Carboxylase System of Escherichia coli

Guchhait, Ras B.; Polakis, S. Efthimios; Dimroth, Peter; Stoll, E.; Moss, Joel; Lane, M. Daniel

doi:10.1016/s0021-9258(19)42203-5

Cited by 195 publications

(36 citation statements)

References 41 publications

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“…These differences are probably caused by the assay method used here. Carboxyltransferase activity was measured in the reverse direction by using transcarboxylation from malonyl-CoA to free biotin methyl ester [8], and might differ from the activity in the true reaction indicated in step 2. Various factors might affect the responsiveness of carboxyltransferase to thiol-reducing and thiol-oxidizing reagents.…”

Section: Discussionmentioning

confidence: 99%

“…The optimal pH values of biotin carboxylase and carboxyltransferase were more basic (pH 8.5) than that of ACCase (pH 8.1). In the physiologically relevant pH range (7)(8), the activity of carboxyltransferase increased more rapidly than that of biotin carboxylase, like that of the ACCase. These results showed that both the biotin carboxylase and carboxyltransferase components in the ACCase were sensitive to pH, and were responsible for the pH dependence of the ACCase.…”

Section: Effects Of Ph On Biotin Carboxylase and Carboxyltransferase Activitiesmentioning

confidence: 97%

“…Biotin carboxylase activity was measured as described elsewhere [8], with a slight modification. In brief, approx.…”

Section: Measurement Of Biotin Carboxylase Activitymentioning

confidence: 99%

“…Carboxyltransferase activity was measured by the reverse reaction method as described elsewhere [8], with a slight modification. The carboxy group transfer from [2-"%C]malonyl-CoA to biotin methyl ester was measured.…”

Section: Measurement Of Carboxyltransferase Activitymentioning

confidence: 99%

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Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component

Kozaki

Sasaki

1999

Biochemical Journal

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Plastidic acetyl-CoA carboxylase (ACCase; EC 6.4.1.2), which catalyses the synthesis of malonyl-CoA and is the regulatory enzyme of fatty acid synthesis, is activated by light, presumably under redox regulation. To obtain evidence of redox regulation in vivo, the activity of ACCase was examined in pea chloroplasts isolated from plants kept in darkness (dark-ACCase) or after exposure to light for 1 h (light-ACCase) in the presence or absence of a thiol-reducing agent, dithiothreitol (DTT). The protein level was similar for light-ACCase and dark-ACCase, but the activity of light-ACCase in the absence of DTT was approx. 3-fold that of dark-ACCase. The light-ACCase and dark-ACCase were activated approx. 2-fold and 6-fold by DTT respectively, indicating that light-ACCase was in a much more reduced, active form than the dark-ACCase. This is the first demonstration of the light-dependent reduction of ACCase in vivo. Measurement of the activities of ACCase, carboxyltransferase and biotin carboxylase in the presence and absence of DTT, and the thiol-oxidizing agent, 5, 5'-dithiobis-(2-nitrobenzoic) acid, revealed that the carboxyltransferase reaction, but not the biotin carboxylase reaction, was redox-regulated. The cysteine residue(s) responsible for redox regulation probably reside on the carboxyltransferase component. Measurement of the pH dependence of biotin carboxylase and carboxyltransferase activities in the ACCase suggested that both components affect the activity of ACCase in vivo at a physiological pH range. These results suggest that the activation of ACCase by light is caused partly by the pH-dependent activation of two components and by the reductive activation of carboxyltransferase.

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Section: Discussionmentioning

confidence: 99%

Section: Effects Of Ph On Biotin Carboxylase and Carboxyltransferase Activitiesmentioning

confidence: 97%

“…Biotin carboxylase activity was measured as described elsewhere [8], with a slight modification. In brief, approx.…”

Section: Measurement Of Biotin Carboxylase Activitymentioning

confidence: 99%

Section: Measurement Of Carboxyltransferase Activitymentioning

confidence: 99%

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Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component

Kozaki

Sasaki

1999

Biochemical Journal

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“…L-[3H]Valine (25 mCi/mmol) and NaH14CO3 (56 mCi/mmol) were from Centre d'Etudes Atomiques (Saclay, France). The latter was purified before use (Guchhait et al, 1974). N.m.r.…”

Section: Experimental Chemicalsmentioning

confidence: 99%

Vitamin K-dependent carboxylation. Mechanistic studies with 3-fluoroglutamate-containing substrates

Vidal-Cros

Gaudry

Marquet

1990

Biochemical Journal

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The tripeptides t-butyloxycarbonyl-Xaa-Glu-[3H]Val, where Xaa is either (2R,3S)- or (2R,3R)-3-fluoroglutamate (respectively the erythro and the threo isomer), were synthesized and their behaviour during vitamin K-dependent carboxylation was studied. Neither peptide was carboxylated. The erythro compound gave rise to an HF-elimination product representing 1% of the starting material. This HF elimination did not occur during incubation of the threo compound. The formation of the dehydropeptide, probably by elimination of an F- anion from an intermediate carbanion, favours the ionic pathway for vitamin K-dependent carboxylation.

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Multienzyme Complexes Involved in the Benson–Calvin Cycle and in Fatty Acid Metabolism

Gontero

Lebreton

Graciet

2018

Annual Plant Reviews Online

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Acetyl Coenzyme A Carboxylase System of Escherichia coli

Cited by 195 publications

References 41 publications

Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component

Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component

Vitamin K-dependent carboxylation. Mechanistic studies with 3-fluoroglutamate-containing substrates

Multienzyme Complexes Involved in the Benson–Calvin Cycle and in Fatty Acid Metabolism

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