Pyruvate oxidase types

Hydrophobic species bearing hydrocarbon chains present vitamin B12 or vitamin B6 type activity [5.37]. Such systems lend themselves to inclusion in membrane or micellar media. They thus provide a link with catalysis in more or less organized media such as membranes, vesicles, micelles, polymers [5.39-5.41] (see Section 7.4). Water soluble cyclophanes showing, for example, transaminase [5.42], acetyl transfer [5.43], pyruvate oxidase [5.44] or nucleophilic substitution [5.45] activity have been described. 

Other types of enzymes When no oxidase or dehydrogenase is available for a target analyte, other types of enzymes have been used for biospedfic recognition e.g. for citric acid detection, citrate lyase, and amperometric detection was possible by coupling to two more enzymatic reactions oxaloacetate decarboxylase and pyruvate oxidase, which convert citric add into H2O2 with the latter being monitored amperometrically with an H202 probe. For detection of acetic add, acetate kinase is used, coupled to pyruvate kinase and pyruvate oxidase [34,35]. 

Kwan et al. [27] l-Lactate Yoghurt milk, soda, sport drinks, and healthy supplement Salicylate hydroxylase (SHL), L-lactate dehydrogenase (LDH), and pyruvate oxidase (PyOD)/entrapped by a poly(carbamoyl) sulfonate (PCS) hydrogel on a Teflon membrane Clark-type oxygen electrode ... 

The antidotal properties of BAL arc a.ssociatcd with the property of heavy metals to react with sullliydryl (SH) groups in proteins (e.g., tlie en/.yme pyruvate oxidase) and interfere with their normal function. 1.2-Dilhiol compounds such as BAL compete effectively with such proteins for the metal by reversibly forming metal ring compounds of the following type ... 

R., Schulz, G. E. (1994), The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum, J. Mol. Biol. 237, 315-335. 

Phosphoketolase and a certain type of pyruvate oxidase produce an acetyl phosphate that is a high-energy metabolite and produce ATP by acetate kinase during anaerobic growth of bacteria. 

ALS shows a high degree of primary sequence homology with pyruvate carboxylase and pyruvate oxidase the ubiquinone cofactors of pyruvate oxidase inhibit ALS, and it has been proposed that the ubiquinone-binding site of the ancestral enzyme also is the site of both SMM and imidazolinone binding. Recent evidence suggests, however, that these two types of herbicide interact differently with ALS (a) imidazolinones cause a rapid decrease in the levels of extractable ALS activity in maize, whereas SMM does not and can protect the ALS activity from this in vivo effect of imidazolinones and (b) not all imidazolinone-tolerant cell lines are insensitive to sulfonylureas. Sulfonylureas and imidazolinones do not, however, show synergistic inhibition of maize ALS in vitro. ... 

Abnormalities of the respiratoiy chain. These are increasingly identified as the hallmark of mitochondrial diseases or mitochondrial encephalomyopathies [13]. They can be identified on the basis of polarographic studies showing differential impairment in the ability of isolated intact mitochondria to use different substrates. For example, defective respiration with NAD-dependent substrates, such as pyruvate and malate, but normal respiration with FAD-dependent substrates, such as succinate, suggests an isolated defect of complex I (Fig. 42-3). However, defective respiration with both types of substrates in the presence of normal cytochrome c oxidase activity, also termed complex IV, localizes the lesions to complex III (Fig. 42-3). Because frozen muscle is much more commonly available than fresh tissue, electron transport is usually measured through discrete portions of the respiratory chain. Thus, isolated defects of NADH-cytochrome c reductase, or NADH-coenzyme Q (CoQ) reductase suggest a problem within complex I, while a simultaneous defect of NADH and succinate-cytochrome c reductase activities points to a biochemical error in complex III (Fig. 42-3). Isolated defects of complex III can be confirmed by measuring reduced CoQ-cytochrome c reductase activity. 

Two enzymes are commonly used for amperometric biosensors, namely lactate oxidase (LOD) and lactate dehydrogenase (LDH). It should be noted that, in this instance, LOD refers to the enzyme which catalyses the reaction shown in Fig. 23.4, in which the products are pyruvate and H202. This type of enzyme was formerly assigned the E.C. number 1.1.3.2, but this was confused with lactate monooxygenase (E.C. 1.13.12.4), which is also commonly referred to as type I lactate oxidase [55] or simply lactate oxidase [56] whose products are acetate, C02 and H202. The LOD which catalyses the reaction shown in Fig. 23.4 has also been referred to as type II lactate oxidase [55] following clarification of this point in a published letter [57], current publications refer to this enzyme as E.C. 1.1.3.x. 

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