Lysine malonate

Yeast extract was reported to contain components that are toxic to cyanobacteria [107]. L-lysine and malonic acid completely killed Microcystis viridis at a concentration of 1 and 40 ppm, respectively. Lysine malonate was found to be more toxic than DL-lysine. 

The variety of educts and products of the higher MCRs is illustrated here. Product 72 (Scheme 1.18) is formed from the five functional groups of lysine, benzaldehyde, and tert-butylisocyanide. The synthesis of 73 is achieved with hydrazine, furanaldehyde, malonic acid, and the isocyano methylester of acetic acid, compound 74 results from the reaction of benzylamine, 5-methyl-2-furanaldehyde, maleic acid mono-ethylester, and benzylisocyanide. ° Zhu et al. prepared a variety of related products, such as, 75, from (9-amino-methyl cinnamate, heptanal, and a-isocyano a-benzyl acetamides. 

QCS036 Lysine 3172 Malic acid 3172 Malonic acid 1 3172 Maltose 3172 Mannitol 1 ... 

Slaframine.—Slaframine (37) is produced by the phytopathogen Rhizoctonia leguminicola. It has been known for some time that (37) derives in part from lysine via pipecolic acid (33), which is incorporated intact the earliest bicyclic intermediate identified is (38) (c/. Vol. 5, p. 9 and ref. 2). New results have shown that the two skeletal carbons in (37), and also in the metabolite (36), not accounted for by pipecolic acid, derive from malonate (and acetate).13 The labelling of (37) by, in particular, [2-2H2]acetate was deduced to be of C-2 on the basis of mass spectral evidence (which is not entirely convincing). The acyl-CoA derivative (34) has been suggested as an intermediate in the biosynthesis of (37) and also of (36). It is to be noted that condensation between malonyl-CoA and pipecolic acid (33) to give (34) must be simultaneous with decarboxylation of malonyl-CoA, since two deuterium atoms of acetate are retained at C-2 in (37) (later intermediates with a double-bond to C-2 are also excluded by these results). 

Thus, hypotheses a and c, which demanded participation of a Cg-Cj unit in the biosynthesis of the phenylquinolizidine moiety, have been disproved. The mode of incorporation of lysine and its metabolites has eliminated routes b and d. The accumulative evidence demonstrates that only path e is consistent with all experimental results. This route predicts an extension of the side chain of the phenylpropanoid precursor by a two-carbon unit supplied by a donor such as acetyl- or malonyl-Coenzyme A. The results of the final experiment with [2-14C]malonate were consistent with hypothesis e but inconclusive. 

The action of the lysine-rich polymers was rather selective for OAA, in that pyruvic, malic, malonic, a-ketoglutaric, glucuronic, oxalic, or aspartic acid were not measurably decarboxylated under conditions in which OAA was 90% decarboxylated. Acetoacetic acid was decarboxylated about - 6 as fast as OAA. This selectivity is not in conflict with other reports of decarboxylation of some of these substrates, because conditions of assay have varied rather widely. The rate of decarboxylation may be essentially related to the relative stability of the substrate in question. Two reactions catalyzed separately by different types of thermal polymers describe a sequence, namely OAA pyruvate-> acetate. This sequence can be considered in the context of the beginnings of metabolism (p. 408). 

D, L-Lysine dihydrochloride 23 Diethyl a-(acetylamino)-a-(3-cyanopropyl)malonate (15 g) is dissolved in freshly distilled acetic anhydride (100 ml), platinum dioxide (0.5 g) is added, and hydrogenation carried out at an initial pressure of 3 atm. Absorption is complete in 3 h. The catalyst is removed, and the acetic anhydride is hydrolysed by cautious addition of water (25 ml). The A,A-diacetyllysine is then cleaved by boiling it for 18 h in acetic acid solution containing concentrated hydrochloric acid (d 1.19 100 ml). Evaporation then affords d,l-lysine dihydrochloride (9g, 77%), m.p. 175-180°, which, after dissolution in anhydrous ethanol and precipitation by ether, melts at 187-188°. 

The first biotin-dependent enzyme to be discovered was acetyl-CoA-car-boxylase, which forms malonic acid and is necessary for the synthesis of fatty acids cf. section 8.5.3). It is assumed that biotin is bonded to a 14-Angstrom-long lysine linker, so that it can swing back and forth between two active centres in the enzyme complex. In the first centre, biotin is carboxylated under the consumption of ATP in the second, the carboxylic acid function is transferred. [115,116]... 

The biosynthesis of slaframine (38) and swainsonine (35) in Rhizoctonia leguminicola involves lysine and proceeds via the intermediacy of pipecolic acid. Carbon atoms 2 and 3 have been demonstrated to come from acetate via malonate (Fig. 30.14). The biosynthesis of swainsonine and related compounds in plants does not appear to have been investigated (Elbein and Molyneux, 1987 Harris et al, 1987 Howard and Michael, 1986). 

The general biogenetic route of cocaine and other related alkaloids is shown in Fig. 5.2.1. The fundamental skeleton is formed by the combination of lysine-ornithine derived pyrrolidine and the three- or four-carbon moiety of ace-tate-malonate origin. The acyl part of scopolamine has been demonstrated to be formed from phenylalanine through deamination and skeletal rearrangement (63). 

If instead of malonic acid the ester with a lysine derivative is employed in the rearrangement (see 212), a series of unusual a-amino acids can be prepared stereoselectively (213) [78]. 

Principal characteristics C. intermedius cultures fail to produce HgS in TSI agar, but hydrogen sulfide production is detectable on more sensitive media such as FeClg gelatin or Pb acetate agar lysine is never decarboxylated. About 20 per cent of strains produce indole and 40 per cent ferment sodium malonate [21, 88]. 

Substantial amounts of radioactivity were incorporated into cycloheximide w hen L-methionine-Me- C, acetic acid-1- C, malonic acid-1,3- C and were tested as possible precursors (Kharatyan et al., 1963 VanIk et al., 1964). Lesser amounts of radioactivity were incorporated from succinic acid-1,4- C or propionic acid-1- C. No incorporation of radioactivity was observed from mevalonic acid-2- C, L-glutamic acid-U- C, L-lysine-U- C or citric acid-1,5- C. The degree of incorporation of the individual precursors is shown in Table 4. A detailed description of the degradation procedures has been presented by VanSk and VondrACek (1965). 

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