Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves

Shimakata, Takashi; Stumpf, P.K.

doi:10.1016/0003-9861(82)90323-x

Cited by 76 publications

(36 citation statements)

References 20 publications

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“…Steady-state kinetic experiments (Table 1) gave a K m value of MabA for acetoacetyl-CoA of 1530 µM, which is 6 times the K m of KARs from plants (Sheldon et al, 1992 ;Shimakata & Stumpf, 1982). In contrast, the k cat and the K m for NADPH reported for these proteins are of the same order of magnitude as those measured for MabA (Table 1).…”

Section: Enzymic Activity Of the Maba Proteinmentioning

confidence: 76%

MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II

et al. 2002

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The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are very long-chain fatty acids of the cell envelope specific to Mycobacterium tuberculosis and other mycobacteria. A potential component of FAS-II, the protein MabA (FabG1), was overexpressed and purified. Sedimentation equilibrium analyses revealed that MabA undergoes a dimer to tetramer self-association with a dissociation constant of 22 µM.

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Section: Enzymic Activity Of the Maba Proteinmentioning

confidence: 76%

MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II

et al. 2002

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“…The NADH requirement has recently been shown to be the result of the specificity of chloroplast enoyl-ACP reductase for NADH (22). Generation of NADH could be achieved by PDC activity.…”

Section: Fraction Number Figmentioning

confidence: 99%

Purification and Characterization of the Pea Chloroplast Pyruvate Dehydrogenase Complex

Camp

Randall²

1985

Plant Physiol.

140

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The pyruvate dehydrogenase complex has been purified 76-fold, to a specific activity of0.6 umoles per minute per milligram protein, beginning with isolated pea (Pisum sativum L. var Little Marvel) chloroplasts. Purification was accomplished by rate zonal sedimentation, polyethyleneglycol precipitation, and ethyl-agarose affinity chromatography. Characterization of the substrates as pyruvate, NAD', and coenzyme-A and the products as NADH, C02, and acetyl-CoA, in a 1:1:1 stoichiometry unequivocally established that activity was the result of the pyruvate dehydrogenase complex. Immunochemical analysis demonstrated significant differences in structure and organization between the chloroplast pyruvate dehydrogenase complex and the more thoroughly characterized mitochondrial complex. Chloroplast complex has a higher magnesium requirement and a more alkaline pH optimum than mitochondrial complex, and these properties are consistent with light-mediated regulation in vivo. The chloroplast pyruvate dehydrogenase complex is not, however, regulated by ATP-dependent inactivation. The properties and subcellular localization of the chloroplast pyruvate dehydrogenase complex are consistent with its role of providing acetyl-CoA and NADH for fatty acid synthesis.The pyruvate dehydrogenase complex is a multicomponent system composed ofthe three enzymes, pyruvate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase. The (11,15,16). Phosphorylation (inactivation) of pyruvate dehydrogenase is catalyzed by a tightly associated kinase and dephosphorylation (activation) by a more loosely associated phosphatase (10).The pivotal position of PDC in metabolism has resulted in a vast amount of research on the enzyme from nonplant tissues. By comparison, relatively little is known about plant PDC, and most information that is available concerns the mitochondrial form of the enzyme. The limited knowledge of plastid PDC prompted the current investigation with the purpose ofestablishing the chloroplast enzyme as a true PDC with properties distinct from the mitochondrial enzyme and consistent with its postulated role in chloroplast fatty acid biosynthesis.

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“…Three different FAS complexes participate in the production of C 18 fatty acids in the plastid. They differ in their b-ketoacyl-acyl carrier protein synthase (KAS) condensing enzymes, which have strict acyl chainlength specificities: KASIII (C 2 -C 4 ; Clough et al, 1992), KASI (C 4 -C 16 ) and KASII (C 16 -C 18 ; Shimakata and Stumpf, 1982). The two reductases and the dehydratase have no particular acyl chain-length specificity and are shared by all three plastidial elongation complexes (Stumpf, 1984).…”

Section: Compound Chain Lengthmentioning

confidence: 99%

Plant surface lipid biosynthetic pathways and their utility for metabolic engineering of waxes and hydrocarbon biofuels

2008

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SummaryDue to their unique physical properties, waxes are high-value materials that are used in a variety of industrial applications. They are generated by chemical synthesis, extracted from fossil sources, or harvested from a small number of plant and animal species. As a result, the diversity of chemical structures in commercial waxes is low and so are their yields. These limitations can be overcome by engineering of wax biosynthetic pathways in the seeds of high-yielding oil crops to produce designer waxes for specific industrial end uses. In this review, we first summarize the current knowledge regarding the genes and enzymes generating the chemical diversity of cuticular waxes that accumulate at the surfaces of primary plant organs. We then consider the potential of cuticle biosynthetic genes for biotechnological wax production, focusing on selected examples of wax ester chain lengths and isomers. Finally, we discuss the genes/enzymes of cuticular alkane biosynthesis and their potential in future metabolic engineering of plants for the production of renewable hydrocarbon fuels.

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Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves

Cited by 76 publications

References 20 publications

MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II

MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II

Purification and Characterization of the Pea Chloroplast Pyruvate Dehydrogenase Complex

Plant surface lipid biosynthetic pathways and their utility for metabolic engineering of waxes and hydrocarbon biofuels

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