Substrate oxidations, pathways

Respiratory, or oxidative, metaboHsm produces more energy than fermentation. Complete oxidation of one mol of glucose to carbon dioxide and water may produce up to 36 mol ATP in the tricarboxyHc acid (TCA) cycle or related oxidative pathways. More substrates can be respired than fermented, including pentoses (eg, by Candida species), ethanol (eg, by Saccharomjces), methanol (eg, by Hansenu/a species), and alkanes (eg, by Saccharomjces lipoljticd). 

Polyunsaturated fatty acids pose a slightly more complicated situation for the cell. Consider, for example, the case of linoleic acid shown in Figure 24.24. As with oleic acid, /3-oxidation proceeds through three cycles, and enoyl-CoA isomerase converts the cA-A double bond to a trans-b double bond to permit one more round of /3-oxidation. What results this time, however, is a cA-A enoyl-CoA, which is converted normally by acyl-CoA dehydrogenase to a trans-b, cis-b species. This, however, is a poor substrate for the enoyl-CoA hydratase. This problem is solved by 2,4-dienoyl-CoA reductase, the product of which depends on the organism. The mammalian form of this enzyme produces a trans-b enoyl product, as shown in Figure 24.24, which can be converted by an enoyl-CoA isomerase to the trans-b enoyl-CoA, which can then proceed normally through the /3-oxidation pathway. Escherichia coli possesses a... 

Most in vitro studies of xanthines have centered around the enzyme xanthine oxidase. Bergmann and co-workers 40-4)) have examined the main oxidative pathways in the xanthine oxidase catalyzed oxidation of purines. The mechanism proposed by these workers 41 > is that the enzyme binds a specific tautomeric form of the substrate, regardless of whether or not that form represents the major structure present in solution. It is then proposed that the purine, e.g., xanthine, undergoes hydration at the N7=C8 double bond either prior to or simultaneously with dehydrogenation of the same position. Accordingly, the process would involve either pathway a or b. Fig. 15. Route a would give a lactim form of the oxidized purine, while b would give the cor-... 

Synthesis of PHAMCL from fatty acids such as octanoic acid or from the corresponding alkanes such as octane was first detected in P. oleovorans [119]. The alkanes are oxidized to the fatty acids the latter are activated by thiokinases and then degraded via the fatty acid /1-oxidation pathway. Obviously intermediates of this pathway accumulate under conditions favorable for the synthesis of PHA and are subsequently converted into substrates for the PHA synthase. Many reactions for the conversion of an intermediate of the -oxidation cycle into R-(-)-3-hydroxyacyl-CoA were considered. These were ... 

Lageveen et al. [41] showed that the monomer composition of aliphatic saturated poly(3HAMCL) produced by P. oleovorans is depended on the type of n-alkane used. It appeared that the n-alkanes were degraded by the subsequent removal of C2-units and it was therefore proposed that the /1-oxidation pathway was involved in poly(3HAMCL) biosynthesis. Preusting et al. [42] confirmed these results but also showed that with hexane as substrate some 3-hydroxyoctanoate and 3-hydroxydecanoate were produced, indicating that additional pathways were involved in poly(3HAMCL) biosynthesis (Table 1). 

Many Pseudomonas strains accumulate MCL-PHAs from alkane, alkene, al-kanoate, alkenoate, or alkanol [5,6,14,96]. The composition of the PHAs formed by the pseudomonads of the rRNA homology group I is directly related to the structure of the carbon substrate used [6]. These results suggested that MCL-PHAs are synthesized from the intermediates of the fatty acid oxidation pathway. In almost all pseudomonads belonging to the rRNA homology group I except Pseudomonas oleovorans, MCL-PHA can also be synthesized from acetyl-CoA through de novo fatty acid synthetic pathway [97]. The -oxidation pathway and de novo fatty acid synthetic pathway function independently in PHA biosynthesis. 

The classic oxidizing systems of human myeloperoxidase and horseradish peroxidase were exploited for their well-known abilities to oxidize phenolic substrates. Under conditions of incubations, the following oxidation pathway was defined (155). Peroxidases are first converted to the oxidized... 

Mg+" reacts with alkyl halides in the gas phase via a range of substrate-dependent pathways Not all halides are reactive—examples of unreactive substrates include methyl chloride, vinyl chloride, trichloro and tetrachloro ethylene. Reaction with ethyl chloride proceeds via an elimination reaction (equation 18) followed by a displacement reaction (equation 19). For larger alkyl halides, such as isopropyl chloride, chloride abstraction also occurs (equation 20). For multiply halogenated substrates such as carbon tetrachloride, oxidative reactions occur (equations 21 and 22), although organometallic... 

The primary events are deeply described in the literature [5] and are summarized in Eqs. (la)—(If) for the oxidative pathways in which a substrate Redi is involved ... 

For every step of the P oxidation sequence there is a small family of enzymes with differing chain length preferences.6 7 For example, in liver mitochondria one acyl-CoA dehydrogenase acts most rapidly on M-butyryl and other short-chain acyl-CoA a second prefers a substrate of medium chain length such as n-octanoyl-CoA a third prefers long-chain substrates such as pal-mitoyl-CoA and a fourth, substrates with 2-methyl branches. A fifth enzyme acts specifically on isovaleryl-CoA. Similar preferences exist for the other enzymes of the P oxidation pathway. In Escherichia coli... 

Biosynthesis occurs from 3-hydroxybutyryl-CoA. Some bacteria incorporate other P-hydroxyac-ids into the polymer.f Apparently various hydroxy-acyl-CoAs can be diverted from the P oxidation pathway to polymer synthesis, and synthases that will accept a variety of P-hydroxyacyl-CoA substrates have been isolated. h i More than 80 different hydroxyacyl groups can be incorporated into the polymer.1 A bacterially produced copolymer of P-... 

Moreover, in the ordered Au monolayer and bilayer structures described above, the Ti4 + of the support titania is not accessible to the reactants, since each surface Ti site binds directly to a Au atom located at the topmost surface. The high catalytic activities for CO oxidation observed on ordered bilayer Au thus strongly suggest a Au-only CO oxidation pathway. The electronic nature of very small Au NPs and thin layers can be assumed to be significantly influenced by the nature and direct involvement of the Ti02 support and the Mo metal substrate, especially the availability of defect sites [26, 27, 88, 89]. 

During cooxidation, some substrates are activated to become more toxic than they were originally. In some cases substrate oxidation results in the production of free radicals, which may initiate lipid peroxidation or bind to cellular proteins or DNA. Another activation pathway involves the formation of a peroxyl radical from subsequent metabolism of prostaglandin G2. This reactive molecule can epoxidize many substates including polycyclic aromatic hydrocarbons, generally resulting in increasing toxicity of the respective substrates. 

Based on his own experimental results and their analysis, Traube has made the correct (in terms of modem understanding) conclusion that H202 displays high reactivity in the presence of a catalyst in the system. This is the pathway of various substrate oxidations by hydrogen peroxide, proceeding in the Fenton system (iron ion + H202), and some biochemical processes. 

The inherent substrate specificities of Pseudomonas sp. 61-3 PHA synthases (PhaClPs and PhaC2Ps) are rather low toward 3HB monomer (17,18), and the fad mutant E. coli strain used in our study cannot generate enough 3HB monomers from the (3-oxidation pathway (21,26). Therefore, we introduced the R. eutropha phaABRe genes to generate enough more 3HB... 

Enzymic oxidation pathways vary with the substrate molecule, for purine-6-thione (60), although being fully oxidized to 6-thiouric acid (62), undergoes displacement first at the 8-carbon (61) rather than at... 

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