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Pyruvate from tryptophan

Alkaloids from tryptophan. The alkaloid harmine, which is found in several families of plants, can be formed from tryptophan and acetaldehyde (or pyruvate) in the same manner as is indicated for the formation of papaverine in Fig. 25-10. Some other characteristic plant metabolites such as psilocybine, an hallucinogenic material from the mushroom... [Pg.1447]

Brevicolline.—The /3-carboline part of the plant alkaloid brevicolline (114) has been shown to derive from tryptophan (94) and pyruvic acid.37 Putrescine (4) and related compounds provide the pyrrolidine ring.38 A key intermediate in brevicolline biosynthesis is likely to be (113), derived by oxidative decarboxylation of (111), which in turn is formed through the condensation of (94) with pyruvic acid condensation of (113) and (112) (formed from putrescine) would lead to (114). This has been supported by successfully mimicking the biogenetic sequence, starting with the chemical oxidative decarboxylation of (111).39... [Pg.20]

Hoshino et al. described that in cultures of Chromobacterium violaceum, lycogalic acid (35, = chromopyrrolic acid) was derived from tryptophan [18]. It was therefore assumed that lycogalic acid (35) was formed by oxidative dimerization of 3-(indol-3-yl)pyruvic acid followed by reaction of the resulting 1,4-dicarbonyl intermediate with an equivalent of ammonia. On the basis of this idea, lycogarubin C (33) was synthesized from methyl 3-(indol-3-yl)pyruvate (37) in a simple one-pot process (Scheme 4). [Pg.231]

INDOLMYCIN (20) is formed from pyruvate, and two enzymes active in initial stages of Its biosynthesis have been studied. They are a transaminase and aC-methyltransferase. The hypothetical route to indolmycin is by indole pyruvate, 3-methyl-indolepyruvate, indolmycenic acid (reduced alpha oxo group) and finally indolmycin which probably takes its amidine group from an arginine molecule 79. The closely related [pyrrolo (1,4) benzodiazepines] 80>81,82 antitumor antibiotics, anthramycin, tomaymycin and sibiromycin are formed from tryptophan (via the kynurenine pathway ), tyrosine and methionine-derived methyl groups 80.si.sz. [Pg.135]

Scission of the side chain leaves an Ai ion which takes up a pioton to give indole from tryptophan (as with tryptophanase) or phenol from tyrosine (as with 3-tyrosinase). The side chain of the original molecule is left as the pyridoxal phosphate complex of aminoacrylic acid, and on hydrolysis the aminoacrylic acid tautomerizes to the imine of pyruvic acid which is hydrolyzed to pyruvic acid and ammonia ... [Pg.93]

Our laboratory has studied the stereochemistry of methyl group formation in a number of a, 0 elimination reactions of amino acids catalyzed by pyridoxal phosphate enzymes. The reactions include the conversions of L-serine to pyruvate with tryptophan synthase 02 protein (78) and tryptophanase (79), of L-serine and l-tyrosine with tyrosine phenol-lyase (80), and l-cystine with S-alkylcysteine lyase (81). In the latter study, the stereospecific isotopically labeled L-cystines were obtained enzymatically by incubation of L-serines appropriately labeled in the 3-position with the enzyme O-acetyl serine sulfhy-drase (82). The serines tritiated in the 3-position were prepared enzymatically starting from [l-3H]glucose and [l-3H]mannose by a sequence of reactions of known stereochemistry (81). The cysteines were then incubated with 5-alkyl-cysteine lyase in 2H20 as outlined in Scheme 19. The pyruvate was trapped as lactate, which was oxidized with K2Cr202 to acetate for analysis. Similarly, Cheung and Walsh (71) examined the conversion of D-serine to pyruvate with... [Pg.277]

The approaches that have been described in some detail for tryptophan synthase may be applied to other PLP-dependent enzymes. Tryptophan indole lyase, or tryptophanase, catalyzes the PLP-dependent P-elimination of indole from tryptophan to yield indole, pyruvate, and NH4+ (Equation 4). [Pg.227]

Although a great number of alkaloids having a /8-carboline structure have been found in nature, very few reports have been published about their biogenesis, and these are concerned only with the plant material. From among the alkaloids mentioned above only harman (180) and 4,5-dihydrocanthin-6-one (181) were demonstrated in feeding experiments with H- and C-labeled precursors to be derived biosynthetically from tryptophan. In the case of harman, tryptamine is probably condensed with pyruvic acid to give l-methyl-l,2,3,4-tetrahydro-j8-carboline-l-carboxylic... [Pg.232]

The chemical structure of heteroauxin was established to be indole-3-acetic acid (indole-P-acetic acid (lAA)). It is considered that lAA is formed by the enzymatic oxidation of indole-3-acetaldehyde derived from tryptophan via indole-3-pyruvic acid or tryptamine. Between these two routes, the main route is thought to be through indole-3-pyruvic acid. [Pg.65]

This enzyme [EC 4.1.3.27] catalyzes the reaction of chorismate with glutamine to generate anthranilate, pyruvate, and glutamate. In certain species, this enzyme is part of a multifunctional protein together with one or more other components of the system for the biosynthesis of tryptophan (Le., indole-3-glycerol-phosphate synthase, anthranilate phosphoribosyltransferase, tryptophan synthase, and phosphoribosylanthranilate isomerase). The anthranilate synthase that is present in these complexes has been reported to be able to utilize either glutamine or ammonia as the nitrogen source. However, it has also been reported that when anthranilate synthase is separated from this complex, only ammonia can serve as a substrate. [Pg.60]

This enzyme [EC 4.1.99.1], also known as L-tryptophan indole-lyase, catalyzes the hydrolysis of L-tryptophan to generate indole, pyruvate, and ammonia. The reaction requires pyridoxal phosphate and potassium ions. The enzyme can also catalyze the synthesis of tryptophan from indole and serine as well as catalyze 2,3-elimination and j8-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. [Pg.688]

The pyruvate dehydrogenase complex from Escherichia coli is considerably more complex than tryptophan synthetase. It has a molecular weight of approximately 4.6 millon and contains three enzymes pyruvate dehydrogenase (Et), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3).82 The overall reaction catalyzed by the complex is... [Pg.201]

Overall, the biosynthesis of 160 is characterized by the dimerization of 168 to give the central structure of the molecule. This head-to-tail dimerization strategy is efficient, using the same substrate twice, and is a sensible route, given the existence of the shikimate pathway, which provides, in turn, a precursor to 168. An analogous dimerization route can be seen for the biosynthesis of K252c (1), described in Sect. 5, where two molecules of indole-3-pyruvic acid imine (125), derived in turn from L-tryptophan (123), are dimerized to give an intermediate that leads to chromopyrrolic acid (128). In both cases, the monomer precursors, either 168 or 125, serve as both nucleophiles and electrophiles, and are activated to react by the presence of the appropriate enzymes. [Pg.185]

The aromatic amino acids, phenylalanine, tryptophan, and tyrosine, are all made from a common intermediate chorismic acid. Chorismic acid is made by the condensation of erythrose-4-phosphate and phosphoenol pyruvate, followed by dephosphorylation and ring closure, dehydration and reduction to give shikimic acid. Shikimic acid is phosphorylated by ATP and condenses with another phosphoenol pyruvate and is then dephosphorylated to give chorismic acid. [Pg.86]

It is of interest to compare the tertiary structure of AspAT with that of other PLP-dependent enzymes. Some PLP enzymes whose primary structures are quite different from AspAT exhibit similar tertiary structures. Such enzymes are a>-amino acid pyruvate aminotransferase,341 phosphoserine aminotransferase351 and tyrosine-phenol lyase361 (Phillips, R., personal communication). Similarity in tertiary structure among these PLP enzymes may lead to the idea that many PLP-dependent enzymes share the same ancestor protein. There are PLP enzymes belonging to its own category, such as glycogen phosphorylase and tryptophan synthase.37 381 These enzymes do not share any similarities in either primary or tertiary structures with AspAT. [Pg.94]

Fig. 7.6 Mechanism of -replacement and /3-elimination reactions with L-serine (X =OH-) or /S-chloro-L-alanine (X- = Cl-). Formation of the Schiff base intermediate with the amino acid ES 1 is followed by removal of the a-proton (H ) and of the leaving group (X-) to form the Schiff base of amino acrylate ES III, the key intermediate in both types of reaction. ES III can be hydrolyzed to pyruvate and NH3 (/3-elimination) or can add the indole cosubstrate (RH) to form the Schiff base of the quinonoid of L-tryptophan ES IV (/3-replacement). Protonation of ES IV leads to release of L-tryptophan. ES IV can also be formed in the reverse direction from L-tryptophan. Fig. 7.6 Mechanism of -replacement and /3-elimination reactions with L-serine (X =OH-) or /S-chloro-L-alanine (X- = Cl-). Formation of the Schiff base intermediate with the amino acid ES 1 is followed by removal of the a-proton (H ) and of the leaving group (X-) to form the Schiff base of amino acrylate ES III, the key intermediate in both types of reaction. ES III can be hydrolyzed to pyruvate and NH3 (/3-elimination) or can add the indole cosubstrate (RH) to form the Schiff base of the quinonoid of L-tryptophan ES IV (/3-replacement). Protonation of ES IV leads to release of L-tryptophan. ES IV can also be formed in the reverse direction from L-tryptophan.
Thus we designed and synthesized a bicyclic pyridoxamine derivative carrying an oriented catalytic side arm (16) [11], Rates for conversion of the ketimine Schiff base into the aldimine, formed with 26 (below) and a-ketovaleric acid, indolepyruvic acid, or pyruvic acid, were enhanced 20-30 times relative to those carried out in the presence of the corresponding pyridoxamine derivatives without the catalytic side arm. With a-ketovaleric acid, 16 underwent transamination to afford D-norvaline with 90% ee. The formation of tryptophan and alanine from indolepyruvic acid and pyruvic acid, respectively, showed a similar preference. A control compound (17), with a propylthio group at the same stereochemical position as the aminothiol side arm in 16, produced a 1.5 1 excess of L-norvaline, in contrast to the large preference for D-amino acids with 16. Therefore, extremely preferential protonation seems to take place on the si face when the catalytic side arm is present as in 16. [Pg.42]


See other pages where Pyruvate from tryptophan is mentioned: [Pg.10]    [Pg.10]    [Pg.1446]    [Pg.21]    [Pg.327]    [Pg.5006]    [Pg.1459]    [Pg.5005]    [Pg.569]    [Pg.636]    [Pg.504]    [Pg.243]    [Pg.231]    [Pg.525]    [Pg.65]    [Pg.178]    [Pg.120]    [Pg.272]    [Pg.770]    [Pg.1059]    [Pg.229]    [Pg.579]    [Pg.176]    [Pg.364]    [Pg.112]    [Pg.54]    [Pg.432]    [Pg.16]   
See also in sourсe #XX -- [ Pg.349 ]




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