Biochemical and molecular biological characterization of plant acetyl-CoA carboxylases

Caffrey, James L.

doi:10.31274/rtd-180813-10069

Cited by 1 publication

(7 citation statements)

References 49 publications

(69 reference statements)

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“…Both the heteromeric and homomeric ACCase are found among higher plants (Sasaki 1995). A homomeric ACCase has been found in the cytosol of every plant studied (Caffrey 1995), with soybean (Anderson 1995(Anderson , 1996 and Arabidopsis (Yanai 1995) containing multiple cytosolic enzymes. The plastidic pool of malonyl-CoA is generated from a separate isoform.…”

Section: Plant Acetyl-coa Carboxylase Forms and Their Genesmentioning

confidence: 99%

“…One possible mechanism for this process is suggested by the maize genome. The plastidic homomeric AC Case was apparently generated from a gene duplication of the cytosolic enzyme that over time became targeted to the plastid (Caffrey 1995). Once the nuclear encoded homomeric form was present in the plastid there may have been less selective pressure to maintain the plastidic heteromeric form; eventually these genes were lost as the homomeric enzyme took over completely for the heteromeric form (Choi 1995).…”

Section: Evolutionary Origins Of Plant Acetyl-coa Carboxylasementioning

confidence: 99%

“…This plastidic isozyme is also much more abundant within the plant then the cytosolic isoform (Egli 1993). The plastidic ACCase found in many dicots, such as Arabidopsis (Choi 1995), spinach (Kanangara 1972, Mohan 1980, tobacco (Shorrosh 1995(Shorrosh ,1996, and in some monocots, such as leek (Caffrey 1995), and barley (Kanangara 1975, Reizel 1976, is of the heteromeric form. The heteromeric form is sometimes referred to as prokaryotic due to its similarity to the ACCase found in the bacterium E. coli.…”

Section: Plastidic Acetyl-coa Carboxylasementioning

confidence: 99%

“…Wheat and rice have been demonstrated to lack the accD homolog, while maize lacks both the accD and cacl homologs (Nagano 1991, Sasaki 1993, Choi 1995. Partial cDNAs have been used to map the maize cytosolic and plastidic homomeric ACCases to separate nuclear chromosomes (Caffrey 1995)…”

Section: Plastidic Acetyl-coa Carboxylasementioning

confidence: 99%

“…While the plastidic form of ACCase may vary between species the cytosolic form has been consistently identified as being a homomeric isoform in species as varied as alfalfa ,Arabidopsis (Yanai 1995), maize (Egli 1993), pea (Alban 1994), soybean (Caffrey 1995, Anderson 1995, and wheat (Gornicki 1994). When the cytosolic protein is isolated from plants like maize, pea, soybean, or the algae Cyclotella cryptica it is found to consist of multifunctional polypeptide subunits ranging from about 230 to 265 kDa in size (Slabas 1985, Charles 1985, Hellyer 1986, Roesler 1993, Egli 1993, Alban 1994, Ashton 1994, Yanai 1995).…”

Section: Cytosolic Acetyl-coa Carboxylasementioning

confidence: 99%

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Expression of acetyl-CoA carboxylase promoter: GUS fusions in developing Arabidopsis thaliana

Rozema¹

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Acetyl-CoA Carboxylase (ACCase) catalyzes the reaction of acetyl-CoA and bicarbonate in order to form malonyl-CoA, which in turn is used as a precursor of many biologically important chemicals (Choi 1995). The significance of this reaction can be demonstrated by the fact that nearly all organisms contain some form of this enzyme, many even contain multiple genes or isoforms. One of the reasons for the widespread presence of ACCase is that the conversion of acetyl-CoA to malonyl-CoA is the first committed step in the production of fatty acids , Wakil 1983. The fatty acids may then be utilized for membranes, structural or protective very long chain fatty acids, or as energy storage.Within bacteria, animal, and fungal cells this is the primary use for malonyl-CoA; plants, however, also use the malonyl-CoA to produce a range of secondary products (Conn 1981. The division of the synthesis of fatty acids and secondary products in plants corresponds to the presence of separate pools of malonyl-CoA within the cytosol and the plastid of the plant cell, whose membranes are impermeable to malonyl-CoA. Since different products are made from the two pools of malonyl-CoA it make sense for the plant to regulate them independently. One way that most plants seem to regulate ACCase and the malonyl-CoA produced is by utilizing isozymes, enzymes encoded by separate genes that differ structurally but have similar functions. Since bacteria, animals, and fungi only have a cytosolic pool of malonyl-CoA they only require a cytosolic ACCase, however, plants are 2 much more complex. Plants contain both a cytosolic and plastidic form of ACCase. The plant's cytosolic isozyme is similar to that found in the animal and fungal kingdoms, and is encoded for by a small gene family. Depending on the plant species, the plastidic isozyme may be similar to the cytosolic form or it may be closer to the ACCase found in bacteria like E. coli (Sasaki 1993, Alban 1994, Konishi 1994). This variability suggests a complex genetic evolution of ACCase within the plant kingdom (Sasaki 1995). In addition to the genetic complexity, the transcription and activation of ACCase allows for more levels ofregulation, which are only beginning to be understood. Acetyl-CoA carboxylase reactionACCase is a member of the biotin containing family of enzymes, a group of enzymes that all require the attachment of a biotin co-factor in order to transfer a carboxyl group between substrates (Knowles 1989). The similarities between ACCase and the other members of this family, such as propionyl-CoA carboxylase, pyruvate carboxylase, 3methylcrotonyl-CoA carboxylase, oxaloacetate decarboxylase, glutaconyl-CoA carboxylase, and transcarboxylase (Caffrey 1995), suggest a common ancestry (Samols 1988), however only some, including ACCase, are widespread in modem organisms. In this group of enzymes biotin is covalently bound to a lysine side chain to form biocytin. From a kinetic standpoint the reaction proceeds in two major steps: first is biotin carboxylation to produce carboxyl-biocytin, ...

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Section: Plant Acetyl-coa Carboxylase Forms and Their Genesmentioning

confidence: 99%

Section: Evolutionary Origins Of Plant Acetyl-coa Carboxylasementioning

confidence: 99%