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Yeast mechanism

Biochemistry resulted from the early elucidation of the pathway of enzymatic conversion of glucose to ethanol by yeasts and its relation to carbohydrate metaboHsm in animals. The word enzyme means "in yeast," and the earfler word ferment has an obvious connection. Partly because of the importance of wine and related products and partly because yeasts are relatively easily studied, yeasts and fermentation were important in early scientific development and stiU figure widely in studies of biochemical mechanisms, genetic control, cell characteristics, etc. Fermentation yeast was the first eukaryote to have its genome elucidated. [Pg.366]

Other Nitrogen Compounds. The basis of the sophisticated nitrogen compounds Hsted in Table 10 is the reaction of formaldehyde with amino compounds. A significant amount of Hterature details investigation of the mechanism of action, particularly whether or not the antimicrobial activity depends on decomposition to formaldehyde (40—42). These compounds tend to have substantial water solubiUty and are more effective against bacteria than fungi and yeasts. Key markets for these compounds are metalworking fluids, cosmetics, and in-can preservation of paints (see Alkanolamines Amines, fatty amines). [Pg.99]

Biosynthetic Mechanism. Riboflavin is produced by many microorganisms, m( dtm. A.shhyagossjpii A.sperigiUus sp remothecium ashbyii Candida yeasts, Debaryomjces yeasts, Hansenu/a yeasts, Picbia yeasts, A. tobactor sp, Clostridium sp, and Bacillus sp. [Pg.77]

The pathways for thiamine biosynthesis have been elucidated only partiy. Thiamine pyrophosphate is made universally from the precursors 4-amino-5-hydroxymethyl-2-methylpytimidinepyrophosphate [841-01-0] (47) and 4-methyl-5-(2-hydroxyethyl)thiazolephosphate [3269-79-2] (48), but there appear to be different pathways ia the eadier steps. In bacteria, the early steps of the pyrimidine biosynthesis are same as those of purine nucleotide biosynthesis, 5-Aminoimidazole ribotide [41535-66-4] (AIR) (49) appears to be the sole and last common iatermediate ultimately the elements are suppHed by glycine, formate, and ribose. AIR is rearranged in a complex manner to the pyrimidine by an as-yet undetermined mechanism. In yeasts, the pathway to the pyrimidine is less well understood and maybe different (74—83) (Fig. 9). [Pg.92]

FIGURE 19.24 A mechanism for the phosphoglycerate mutase reaction in rabbit muscle and in yeast. Zelda Rose of the Institute for Cancer Research in Philadelphia showed that the enzyme requires a small amount of 2,3-BPG to phosphorylate the histidine residue before the mechanism can proceed. Prior to her work, the role of the phosphohistidine in this mechanism was not understood. [Pg.627]

Based on the action of thiamine pyrophosphate in catalysis of the pyruvate dehydrogenase reaction, suggest a suitable chemical mechanism for the pyruvate decarboxylase reaction in yeast ... [Pg.672]

Fermenting baker s yeast also catalyzes the 1,4-addition of a formal trifluoroethanol-d1-synthon to a,/i-unsaturated aldehydes, to give optically active l,l,l-trifluoro-2-hydroxy-5-alka-nones52. Presumably, the mechanism involves oxidation of the alcohol to the corresponding aldehyde followed by an umpolung step with thiamine pyrophosphate and Michael addition to the a,/i-unsaturated aldehyde. For example, l,l,l-trifluoro-2-hydroxy-5-hexanone (yield 26%, ee 93%) is thus obtained from trifluoroethanol and l-bnten-3-one. [Pg.677]

Keaveney M, Struhl K Activator-mediated recruitment of the RNA polymerase machinery is the predominant mechanism for transcriptional activation in yeast. Mol Cell 1998 1 917. Lemon B, Tjian R Orchestrated response a symphony of transcription factors for gene control. Genes Dev 2000 l4 255l. Maniatis T, Reed R An extensive network of coupling among gene expression machines. Nature 2002 416 499. [Pg.357]

Stevens SW et al Composition and functional characterization of the yeast spliceosomal penta-snRNP. Mol Cell 2002 9 31-Tucker M, Parker R Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae. Ann Rev Biochem 2000 69 571. [Pg.357]

Biochemical and genetic experiments in yeast have revealed that the b poly(A) tail and its binding protein, Pablp, are required for efficient initiation of protein synthesis. Further studies showed that the poly(A) tail stimulates recruitment of the 40S ribosomal subunit to the mRNA through a complex set of interactions. Pablp, bound to the poly(A) tail, interacts with eIF-4G, which in turn binds to eIF-4E that is bound to the cap structure. It is possible that a circular structure is formed and that this helps direct the 40S ribosomal subunit to the b end of the mRNA. This helps explain how the cap and poly(A) tail structures have a synergistic effect on protein synthesis. It appears that a similar mechanism is at work in mammalian cells. [Pg.365]

The yeast strain SCPP exhibits all of the panoply required for the degradation of pectins from various sources. This enzymatic machinery is secreted into the growth medium. Hence, we developped interest on the regulatory mechanisms controlling the synthesis of the main activity produced by the SCPP strain, i.e. the polygalacturonase. [Pg.739]

A rather satisfactory explanation of the irreversibility of amino acid accumulation in yeast cells is that it might result from specific regulatory mechanisms capable of immobilizing the transporters in a closed position. Uptake of amino acids by a number of permeases does indeed appear to be regulated by specific, and possibly allosteric, feedback inhibition. This idea is based on the fact that a number of transport systems seem to be specifically inhibited by their internally accumulated... [Pg.232]

Although single-electron-transfer (SET) processes would be expected to be important in reactions that use metals as reagents, this type of process has also been recognized in the reduction of carbonyl groups that involve 1,4-dihydronicotinamide derivatives . Recent work by Oae and coworkers" has shown that an SET process is operative in the reduction of dibenzothiophene S-oxide by l-benzyl-l,4-dihydronicotinamide when the reaction is catalyzed by metalloporphins. The reaction is outlined in equation (18), but the study gave results of much more mechanistic than synthetic value. This type of study is relevant to understanding biochemical mechanisms since it is known that methionine sulphoxide is reduced to methionine by NADPH when the reaction is catalyzed by an enzyme isolated from certain yeasts . [Pg.933]


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See also in sourсe #XX -- [ Pg.538 ]




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