Propionyl-CoA carboxylase in Nocardia mediterranei

Gygax, D

doi:10.1016/0378-1097(84)90211-8

Cited by 2 publications

(5 citation statements)

References 10 publications

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“…Interestingly, A. brierleyi acyl-CoA carboxylase had a K m for propionyl-CoA that was only 1.6 times lower than its K m for acetyl-CoA. This result differs from those for other organisms, in which the K m for propionyl-CoA was 3-to 14-fold lower than the K m for acetyl-CoA (15,17,27,39,46). These findings imply the real in vivo bifunctional characteristics of acetyl-CoA carboxylase and propionyl-CoA carboxylase in the modified 3-hydroxypropionate cycle.…”

Section: Discussionmentioning

confidence: 79%

“…Moreover, the kinetic parameters of the purified enzyme indicated that acyl-CoA carboxylase had the specific activities of acetyl-CoA and propionyl-CoA carboxylases equally, and the K m for acetyl-CoA was only 1.6 times higher than the K m for propionyl-CoA. Both propionyl-CoA carboxylase from Nocardia mediterranei (15) and acyl-CoA carboxylase from M. tuberculosis, M. bovis (46), and Propionibacterium shermanii (62) also had acetyl-CoA and propionyl-CoA carboxylase activities. Therefore, our results would suggest that the position of the A. brierleyi acyl-CoA carboxylase should be between those of propionyl-CoA carboxylase and the bacterial type of acetyl-CoA carboxylase and also that the enzyme should be named as an acyl-CoA carboxylase.…”

Section: Discussionmentioning

confidence: 97%

“…These enzymes have been purified and characterized from plants (44, 48), animals (36, 38, 58, 64, 67), yeast (39), algae (52, 69), and bacteria (9,15,17,27,46,62). To our knowledge, however, no report of the purification of acetyl-CoA carboxylase or propionyl-CoA carboxylase from Archaea has been published.…”

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confidence: 99%

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Characterization of a Bifunctional Archaeal Acyl Coenzyme A Carboxylase

et al. 2003

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Acyl coenzyme A carboxylase (acyl-CoA carboxylase) was purified from Acidianus brierleyi. The purified enzyme showed a unique subunit structure (three subunits with apparent molecular masses of 62, 59, and 20 kDa) and a molecular mass of approximately 540 kDa, indicating an ␣ 4 ␤ 4 ␥ 4 subunit structure. The optimum temperature for the enzyme was 60 to 70°C, and the optimum pH was around 6.4 to 6.9. Interestingly, the purified enzyme also had propionyl-CoA carboxylase activity Acidianus brierleyi is a facultatively anaerobic, thermoacidophilic, sulfur-metabolizing archaeon that can grow either heterotrophically or autotrophically at an optimum temperature around 70°C and an optimum pH of 1.5 to 2 (18). Under autotrophic growth, this archaeon utilizes the modified 3-hydroxypropionate cycle for CO 2 fixation (21). The 3-hydroxypropionate cycle was originally proposed for a filamentous green non-sulfur-photosynthetic bacterium, Chloroflexus auranticus (63), and has recently been found in the archaea A. brierleyi (21), Metallosphaera sedula, Sulfolobus metallicus, and Acidianus infernus (37). The enzymes for the CO 2 fixation of this cycle are acetyl coenzyme A carboxylase (acetyl-CoA carboxylase) and propionyl-CoA carboxylase. Acetyl-CoA carboxylase catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA, whereas propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA to form methylmalonyl-CoA. Although some enzymes in the 3-hydroxypropionate cycle, namely, malonyl-CoA reductase (20) and propionyl-CoA synthase (1), were recently purified from C. auranticus and characterized, the key carboxylating enzymes of this cycle have not been purified yet.Acetyl-CoA carboxylase and propionyl-CoA carboxylase have been known to be involved in fatty acid biosynthesis (41) and the synthesis of secondary metabolites (51), respectively. These enzymes have been purified and characterized from plants (44, 48), animals (36, 38, 58, 64, 67), yeast (39), algae (52, 69), and bacteria (9,15,17,27,46,62). To our knowledge, however, no report of the purification of acetyl-CoA carboxylase or propionyl-CoA carboxylase from Archaea has been published. We report here the purification and molecular characterization of the acyl-CoA carboxylase from A. brierleyi, which plays an important role in the modified 3-hydroxypropionate cycle. Particularly, the bifunctional character of the enzyme (acetyl-CoA carboxylase and propionyl-CoA carboxylase) has been reported. Some characteristics of the enzyme have been shown to be unique among the known acetyl-CoA carboxylases.

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Section: Discussionmentioning

confidence: 79%

Section: Discussionmentioning

confidence: 97%

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Characterization of a Bifunctional Archaeal Acyl Coenzyme A Carboxylase

et al. 2003

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“…These amino acids activated propionyl-CoA carboxylase activity of Nocardia mediterranei (Gygax et al 1984). The purified M. xanthus propionylCoA carboxylase activity was not activated by these amino acids.…”

Section: Fig 2 a B Sds-page Andmentioning

confidence: 94%

“…The enzyme is a key enzyme in the catabolic pathway for oddchain fatty acids and branched-chain amino acids (Rosenberg 1983). In some bacteria, propionyl-CoA carboxylase also plays an important role in polyketide and fatty acid synthesis (Hunaiti and Kolattukudy 1982;Gygax et al 1984;Bramwell et al 1996;Kimura et al 1997). Methylmalonyl-CoA formed by propionyl-CoA carboxylase is used for the synthesis of methyl-branched fatty acids and polyketides (Cardinale et al 1970;Dobson et al 1990;Gu et al 1993).…”

Section: Introductionmentioning

confidence: 98%

Propionyl-CoA carboxylase of Myxococcus xanthus : catalytic properties and function in developing cells

Kimura

Kojyo²,

Kimura³

et al. 1998

Archives of Microbiology

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An acyl-coenzyme A carboxylase that carboxylates acetyl-CoA, butyryl-CoA, propionyl-CoA, and succinyl-CoA was purified from Myxococcus xanthus. Since the enzyme showed maximal rates of carboxylation with propionyl-CoA, the enzyme is thought to be propionyl-CoA carboxylase. The apparent Km values for acetyl-CoA, butyryl-CoA, propionyl-CoA, and succinyl-CoA were found to be 0.2, 0. 2, 0.03, and 1.0 mM, respectively. The native enzyme has a molecular mass of 605-615 kDa and is composed of nonidentical subunits (alpha and beta) with molecular masses of 53 and 56 kDa, respectively. The enzyme showed maximal activity at pH 7.0-7.5 and at 25-30 degrees C, and was affected by variation in concentrations of ATP and Mg2+. During development of M. xanthus, the propionyl-CoA carboxylase activity increased gradually, with maximum activity observed during the sporulation stage. Previous work has shown that a propionyl-CoA-carboxylase-deficient mutant of M. xanthus reduces levels of long-chain fatty acids. These results suggest that the propionyl-CoA carboxylase is also responsible for the carboxylation of acetyl-CoA to malonyl-CoA used for the synthesis of long-chain fatty acids during development.

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Propionyl-CoA carboxylase in Nocardia mediterranei

Cited by 2 publications

References 10 publications

Characterization of a Bifunctional Archaeal Acyl Coenzyme A Carboxylase

Characterization of a Bifunctional Archaeal Acyl Coenzyme A Carboxylase

Propionyl-CoA carboxylase of Myxococcus xanthus : catalytic properties and function in developing cells

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