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Formate carbon units, source

Cyclopropanones have been used as unique sources of three-carbon units in various synthetic applications including the synthesis of natural products. In general, the sources of the ketones have been the readily available hemiketals or their derivatives as is illustrated in Scheme 49and in the formation of (-I-)-ll-deoxyprostaglandin E2 methyl ester (Scheme 58) ... [Pg.1523]

The most reduced coenzyme is 5-methyl tetrahydrofolate poly glutamate. It is the source of the methyl group added to homocysteine regenerating methionine and tetrahydrofolate ready to accept a one-carbon unit from formate or serine. This last reaction is where folic acid and vitamin come together (Figs. 8.49, 8.52, and 8.53). The implications of this reaction and how folic acid can mask pernicious anemia are discussed in the seetion on vitamin Big (cyanocobalamin). Note that the formation of 5-methyl-THF nor-mdly is not reversible. Tetrahydrofolate can be regenerated only if there is adequate methyl cobalamin coenzyme. [Pg.407]

Which of the following answers completes the sentence correctly The major source of one-carbon units for the formation of the tetrahydrofolate derivative methylenetetrahydrofolate is the conversion of... [Pg.429]

A variety of thiokinases probably exist, but only a few of them have been identified. Acetic acid and butyryl thiokinase have been purified from a variety of sources, including yeast, liver, and muscle. These two enzymes differ in their specificity for the substrate. Acetic thiokinase catalyzes only the oxidation of propionic, acetic, and acrylic acids, but butyryl thiokinase activates fatty acids of chain lengths ranging from 4-to 12-carbon units. A third thiokinase was also discovered. It acts on fatty acid chains with 5- to 22-carbon units and is found in the microsomes. This intracellular distribution is in striking contrast with the cellular location of all other enzymes involved in fatty acid oxidation, which are all in mitochondria. The palmityl enzyme, which is active in the presence of ATP and CoA, becomes inactive when incubated in the absence of CoA therefore, it has been proposed that the active form of the enzyme involves the formation of an enzyme-CoA complex. The heart, the skeletal muscle, and the kidney also contain a thiokinase that specifically activates acetoacetic acid. Acetoacetic acid thiokinase is absent in liver this observation is significant in the pathogenesis of ketosis. [Pg.55]

Pd-catalyzed reactions of allylic esters such as aUyl acetates, carbonates, and phosphates with soft carbon nucleophiles such as malonate esters are useful for carbon-carbon bond formation (Sects. V.2.1.1-V.2.1.5). hi this section, Pd-catalyzed substitution reactions of nitrogen-containing allylic derivatives such as allylic amines, ammonium salts, tosylim-ides, and nitro compounds are described (Scheme 1). The allylic derivatives of other group 15 atoms have never been used as allyl unit source in Pd-catalyzed alkylation reactions so far. [Pg.184]

The source of one-carbon units for folate One-carbon units at the oxidation level of formate can enter... [Pg.212]

The following examples, found in R. eutropha, illustrate the formation of copolymers (cf. [37]). With propionic acid as an additional carbon source, the 3-ketothiolase catalyzes the condensation of the propionyl-CoA unit with acetyl-CoA to form 3-ketovaleryl-CoA, which is reduced to 3-hydroxyvalerate moieties and polymerized by the synthase [27]. [Pg.129]


See other pages where Formate carbon units, source is mentioned: [Pg.917]    [Pg.289]    [Pg.810]    [Pg.810]    [Pg.1398]    [Pg.810]    [Pg.810]    [Pg.116]    [Pg.193]    [Pg.485]    [Pg.464]    [Pg.301]    [Pg.122]    [Pg.309]    [Pg.216]    [Pg.217]    [Pg.541]    [Pg.1327]    [Pg.256]    [Pg.23]    [Pg.76]    [Pg.739]    [Pg.732]    [Pg.172]    [Pg.90]    [Pg.162]    [Pg.335]    [Pg.777]    [Pg.550]    [Pg.7]    [Pg.733]    [Pg.916]    [Pg.196]    [Pg.947]    [Pg.1039]    [Pg.216]    [Pg.10]    [Pg.42]    [Pg.184]    [Pg.217]   
See also in sourсe #XX -- [ Pg.810 ]

See also in sourсe #XX -- [ Pg.810 ]

See also in sourсe #XX -- [ Pg.810 ]

See also in sourсe #XX -- [ Pg.810 ]




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