Synthesis of Stereospecifically Deuterated Phenylalanines and Determination of Their Configuration

Bartl, Knut; Cavalar, Christiane; Krebs, Traute; Ripp, Engelbert; Rétey, János; Hull, William E.; Günther, Helmut; Simon, Helmut

doi:10.1111/j.1432-1033.1977.tb11246.x

Cited by 26 publications

(7 citation statements)

References 12 publications

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“…The ORD curve of both products turned out to be exact mirror images. The product obtained by hydrogenation with C. sporogenes was identical with that which we prepared with C. La 1 and determined as (2~,3~~-3-pheny~-[2,3-*H]propionate [8,9]. Though the enoate reductases of C. La 1, C. k~~~~e~ and C. sporogenes are different in substrate specificity [7] and physical properties such as isoelectric points, they show an identical stereochemical course.…”

Section: Resultsmentioning

confidence: 74%

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On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius

et al. 1981

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Section: Resultsmentioning

confidence: 74%

“…For the isolation of the 3-phenyl- [2,3-2H]propionic acid see section 1 .c. [8]. For the conversion of (2S,3R)-3-phenyl-[2,3-'H]propionic acid to (3R)-3-phenyl [3-2H]propionic acid 370 mg of the former were boiled for 5 h under nonhydrous conditions in 0.55 ml methanol containing 60 mg sulphuric acid.…”

Section: Methodsmentioning

confidence: 99%

On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius

et al. 1981

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“…The product exhibited a plain negative ORD curve between 400 and 600 nm and contained two vicinal deuterium atoms according to its 'H-NMR spectrum. By analogy to the known stereospecificity of enoate reductase with (E)-cinnamic acid [21] and other unsaturated acids [23] as substrates it follows …”

Section: '5'-dimethoxy-(e)-cinnamic Acid (Compound 1) Wasmentioning

confidence: 99%

“…La 1 [21,24] (Scheme 1). The product exhibited a plain negative ORD curve between 400 and 600 nm and contained two vicinal deuterium atoms according to its 'H-NMR spectrum.…”

Section: '5'-dimethoxy-(e)-cinnamic Acid (Compound 1) Wasmentioning

confidence: 99%

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Steric Course of the NIH Shift in the Enzymic Formation of Homogentisic Acid

Leinberger

Rétey

Hull

et al. 1981

European Journal of Biochemistry

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1. 4-Hydroxyphenylpyruvate dioxygenase has been purified from beef liver to a specific activity of 0.021 U/mg at 25 "C.2. Samples of (3R)-and (35')-4'-hydro~yphenyl[3-~H~]pyruvate were prepared by taking advantage of the known stereospecificity of phenylpyruvate keto -enol-isomerase (tautomerase). These were converted in situ by the dioxygenase into the corresponding deuterium-labelled homogentisic acids, which were isolated as the crystalline 2',5'-diinethyl derivatives after treatment with dimethyl sulphate.3. 2',5'-Dimethoxy-(4-cinnamate was deuterated by enoate reductase from Clostridiurn sp. La 1 to afford (2S, 3R)-3-(2',5'-dimetho~yphenyI)-[2-~H~, propionate which was in turn chemically degraded to (S)-2,5-dimethoxyphenyl r2 Hl lacetic acid. 5. In the 500-MHz 'H-NMR spectrum the 2-methylene protons of unlabelled 2,5-dimethoxyphenylacetic acid (-)-menthy1 ester appeared as a well resolved AB system. Using a triple resonance technique and the reference samples (b) and (c) the 2-HR, atom could be correlated with the high-field half and the 2-HsI atom with the lowfield half of the AB system. 6. By comparison of the spectra of the enzymically obtained samples (d) and (e) with the reference spectra it was concluded that in the dioxygenase reaction the side-chain migration occurred with retention of configuration at the methylene C atom.4-Hydroxyphenylpyruvate dioxygenase is involved in the enzymic degradation of tyrosine and catalyses the following reaction [Eqn (l)] :The oxidative decarboxylation of the substrate is coupled with an ortho shift of the side chain reminiscent of the wellknown NIH shift of the para-hydrogen atom during the hydroxylation of phenylalanine [I, 21. Several mechanisms have been suggested for this remarkable transformation [2 -71, none of them has, however, been proved. By the use of l 8 0 2 it has been shown that both atoms of molecular oxygen are incorporated into the same homogentisic acid molecule thus justifying the name dioxygenase [8].The enzyme has been isolated from mammalian, avian and human liver [9-121 and recently from Pseudoinonas sp. P.J. 874 as well [13]. No specific prosthetic group has been yet detected. However, vitamin C and Fe2+ ions function as activators. In vim the best activator is 2,6-dichlorophenolindophenol in its reduced form [14]. (1 W) was applied over the deuterium lock circuit of the Proton magnetic 312 standard 'H-observe probe head. 'H-homodecoupling at the aromatic protons was performed simultaneously in the conventional fashion. Mass spectra were measured with a Hitachi-Perkin-Elmer RMU-6A spectrograph. The limit of error of the mass spectroscopic measurements was estimated to be 1 %. Optical rotatory dispersion (ORD) measurements were conducted with the polarimeter Jasco V. The circular dichroism (CD) curves were obtained with dichrograph Mark I11 of Jobin-Yvon. For ultraviolet spectroscopic measurements, a Unicam SP-1800 spectrophotometer was used.Dialyses were carried out with a hollow-fiber system model DC 2 of Amicon. MaterialsPhenylpyruvate ke...

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Stereochemistry of Metabolic Reactions of Amino Acids

Young

1994

Topics in Stereochemistry

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Synthesis of Stereospecifically Deuterated Phenylalanines and Determination of Their Configuration

Cited by 26 publications

References 12 publications

On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius

On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius

Steric Course of the NIH Shift in the Enzymic Formation of Homogentisic Acid

Stereochemistry of Metabolic Reactions of Amino Acids

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