Phosphate donor

The charged group introduced into products by the aldol donors (phosphate, carboxylate) facilitates product isolation and purification by salt precipitation and ion exchange techniques. Although many aldehydic substrates of interest for organic synthesis have low water solubility, at present only limited data is available on the stability of aldolases in organic cosolvents, thus in individual cases the optimal conditions must be chosen carefully. 

Phosphorylation and dephosphorylation Phosphorylation reactions are catalyzed by a family of enzymes called protein kinases that use adenosine triphosphate (ATP) as a phosphate donor. Phosphate groups are cleaved from phosphorylated enzymes by the action of phosphoprotein phosphatases (Figure 5.18). 

Transformation to other Types of Glycosyl Donor Phosphate... 

Although the process requires the addition of a phosphate donor, such as glycerol-2-phosphate, it may be a valuable tool for cleaning water contaminated with radionuchdes. An alternative mode of uranium precipitation is driven by sulfate-reducing bacteria such as Desulfovibrio desulfuricans which reduce U(VI) to insoluble U(IV). When combined with bicarbonate extraction of contaminated soil, this may provide an effective treatment for removing uranium from contaminated soil (85). 

Solvating extractants contain one or more electron donor atoms, usually oxygen, which can supplant or partially supplant the water which is attached to the metal ions. Perhaps the best known example of such an extractant is tri-( -butyl) phosphate) [126-73-8] (TBP), which forms... 

The O or S atoms in P=0 and P=S groups may act as electron donors although these groups form relatively weak complexes with electron acceptor compounds such as nonpolarizable, more electropositive (ie, hard) acids, including protons (14). Use is made of this property in the recovery of uranium from wet-process phosphoric acid by extractants such as trioctylphosphine oxide [78-50-2] and di(2-ethylhexyl) hydrogen phosphate [298-07-7]. 

Phosphite triesters, P(OR)3, form donor complexes with transition metals and other acceptors and are oxidized to the respective phosphates under appropriate conditions. 

In the biosynthesis of the thia2ole, cysteine is the common sulfur donor. In yeasts, the C-2 and N may be suppHed by glycine, and the remaining carbons byD-ribulose-5-phosphate [108321-99-9] (50). In anaerobic bacteria, the C-2 andN maybe recmited from tyrosine and the carbons from D-l-deoxyxylulose [16709-34-5] (51), whereas in aerobic bacteria the C-2 and N maybe derived from glycine, as in yeasts 7 (74—76,83—86) (see Fig. 9). 

Figure 7.4 The edges of the base pairs in DNA that ate in the major groove are wider than those in the minor groove, due to the asymmetric-attachment of the base pairs to the sugar-phosphate backbone (a). These edges contain different hydrogen bond donors and acceptors for potentially specific interactions with proteins (b).

FIGURE 14.22 Glutamate aspartate aminotransferase, an enzyme conforming to a double-displacement bisnbstrate mechanism. Glutamate aspartate aminotransferase is a pyridoxal phosphate-dependent enzyme. The pyridoxal serves as the —NH, acceptor from glntamate to form pyridoxamine. Pyridoxamine is then the amino donor to oxaloacetate to form asparate and regenerate the pyridoxal coenzyme form. (The pyridoxamine enzyme is the E form.)... 

Nicotinamide is an essential part of two important coenzymes nicotinamide adenine dinucleotide (NAD ) and nicotinamide adenine dinucleotide phosphate (NADP ) (Figure 18.19). The reduced forms of these coenzymes are NADH and NADPH. The nieotinamide eoenzymes (also known as pyridine nucleotides) are electron carriers. They play vital roles in a variety of enzyme-catalyzed oxidation-reduction reactions. (NAD is an electron acceptor in oxidative (catabolic) pathways and NADPH is an electron donor in reductive (biosynthetic) pathways.) These reactions involve direct transfer of hydride anion either to NAD(P) or from NAD(P)H. The enzymes that facilitate such... 

EDTA, leading to a postulate that more than one equivalent of Ca2+ can be captured by X (e.g. one Ca2+ sequestered by the three amines and the three carboxylates and another Ca2 + by the remaining half the donor groups), as the Dreiding model suggests. The fact that there was no interaction at neutral pH of X with phosphate or oxalate anions was separately confirmed. Thus, the dissolution of Ca3(P04)2 and Ca(C204) is entirely due to the cation complexation mechanism. 

Due to mechanistic requirements, most of these enzymes are quite specific for the nucleophilic component, which most often is dihydroxyacetone phosphate (DHAP, 3-hydroxy-2-ox-opropyl phosphate) or pyruvate (2-oxopropanoate), while they allow a reasonable variation of the electrophile, which usually is an aldehyde. Activation of the donor substrate by stereospecific deprotonation is either achieved via imine/enamine formation (type 1 aldolases) or via transition metal ion induced enolization (type 2 aldolases mostly Zn2 )2. The approach of the aldol acceptor occurs stereospecifically following an overall retention mechanism, while facial differentiation of the aldehyde is responsible for the relative stereoselectivity. 

Similar to DHAP aldolases, the 3-hexulose 6-phosphate aldolase found in Methylomonas Ml 5 is highly specific for the aldol donor component D-ribulose 5-phosphate, but accepts a wide variety of aldehydes as replacement for formaldehyde as the acceptor. With propanal,... 

A subclass of lyases, involved in amino acid metabolism, utilizes pyridoxal 5-phosphate (PLP, 3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinecarbaldehyde) as a cofactor for imine/ enamine-type activation. These enzymes are not only an alternative to standard fermentation technology, but also offer a potential entry to nonnatural amino acids. Serine hydroxymethyl-tansferase (SHMT EC 2.1.2.1.) combines glycine as the donor with (tetrahydrofolate activated) formaldehyde to L-serine in an economic yield40, but will also accept a range of other aldehydes to provide /i-hydroxy-a-amino acids with a high degree of both absolute and relative stereochemical control in favor of the L-erythro isomers41. 

A number of lyases are known which, unlike the aldolases, require thiamine pyrophosphate as a cofactor in the transfer of acyl anion equivalents, but mechanistically act via enolate-type additions. The commercially available transketolase (EC 2.2.1.1) stems from the pentose phosphate pathway where it catalyzes the transfer of a hydroxyacetyl fragment from a ketose phosphate to an aldehyde phosphate. For synthetic purposes, the donor component can be replaced by hydroxypyruvate, which forms the reactive intermediate by an irreversible, spontaneous decarboxylation. 

Most of the PKIs currently in clinical trials are small molecules that compete for the ATP-binding site [3,5]. They prevent the phosphate donor ATP to bind to the protein kinase, and hence the target protein will not become phosphorylated and the perturbed signalling can be terminated. 

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