Amino Acid Derivatives. II. Enzymatic Synthesis of Phenylhydrazides of Carboallyloxyamino Acids<sup>1,2</sup>

Milne, H. Bayard; Stevens, Calvin L.

doi:10.1021/ja01160a091

Cited by 13 publications

(6 citation statements)

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“…Synthesis with D-Leu-NH2 was much slower than that of the L-form. Similar stereospecificity has been observed with papain (Milne & Stevens, 1950). Interestingly, the stereospecificity of papain for anilide or hydrazide synthesis is dependent on the acyl group for blocking the ac-amino group in the donor (Bennett & Niemann, 1950;Schuller & Niec mann, 1951); stringent stereospecificity was observed with CH3COor C6H5CObut less with CH30CO-, C2H5OCOor C6H5CH20CO-.…”

Section: Effects Of the Type Of Donor Esterssupporting

confidence: 58%

α-Chymotrypsin as the catalyst for peptide synthesis

Morihara¹,

Oka²

1977

Biochemical Journal

126

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alpha-Chymotrypsin (EC 3.4.21.1)-catalysed syntheses of peptides were performed with various N-acylated amino acid or peptide esters as donors, and amino acid derivatives, peptides or their derivatives as acceptors. Under optimal conditions the synthesis was almost quantitative. As acceptor nucleophiles, free amino acids or the ester derivatives were inadequate, but amino acid amides or hydrazides, di- or tri-peptides, or the amides, hydrazides and esters of the peptides were useful. The nucleophile specificity for synthesis was markedly similar to the leaving-group specificity in hydrolysis; hydrophobic or bulky amino acid residues were most effecient at both P1' and P2' positions [notation of Schechter & Berger (1967) Biochem. Biophys. Res. Commun. 27, 157-162], but L-proline as well as D-amino acid residues were the worst choices. The synthesis was further dependent on the solubility of the products synthesized; a higher yield of products was expected with lower solubility. As donor esters, good substrates were all useful. Accordingly, fragment condensation was possible by using N-acylated peptide esters and various peptides. The present study suggested that alpha-chymotrypsin may become a useful tool for peptide synthesis.

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Section: Effects Of the Type Of Donor Esterssupporting

confidence: 58%

α-Chymotrypsin as the catalyst for peptide synthesis

Morihara¹,

Oka²

1977

Biochemical Journal

126

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“…The analytical sample melted at 192-193°. Ultraviolet: 218 (28,400); 277 (7,450) (2) With ammonium phosphate. A mixture of 7.2 g. (0.05 mole) of indole-3-aldehyde, 7.2 g. (0.054 mole) of dibasic ammonium phosphate, 25 ml.…”

Section: Experimental29mentioning

confidence: 99%

The Synthesis of α-Methyltryptophans and α-Alkyltryptamines

Heinzelman¹,

Anthony²,

Lyttle³

et al. 1960

J. Org. Chem.

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“…(2) to determine the effect of variation and location of substituent on substituted benzhydrazides in these reactions; (3) to resolve racemic acylated amino acids by means of papain in reactions with hydrazides; (4) to attempt to resolve DL-mandelic hydrazide in its reaction with hippuric acid, a noilasymmetric acylated amino acid; (5) to attempt a partial asymmetric synthesis in the reaction between ethylmalonic hydrazide and carbobenzoxyglycine.…”

mentioning

confidence: 99%

“…The Biogenesis of Morphine1 By Edward Leete Received January 5,1959 Radioactive morphine was obtained when DL-phenylalanine-2-C14 or DL-tyrosine-2-C14 was fed to Papaver somniferum plants. Systematic degradation of the morphine derived from the tyrosine yielded compounds whose activities were compatible with the hypothesis that morphine is formed from two molecules of tyrosine via norlaudanosine.…”

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confidence: 99%

Resolutions and an Attempted Partial Asymmetric Synthesis in Papain-Catalyzed Syntheses of N^α,N^β-Diacylhydrazines from Hydrazides and Acylated Amino Acids

Abernethy¹,

Kientz²,

Johnson³

et al. 1959

J. Am. Chem. Soc.

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N",N0-Diacylhydrazities have been prepared successfully from hydrazides and acylated amino acids by papain catalysis. In every reaction where racemic acylated amino acids were employed, resolution occurred. The optimum pH for the reaction between benzhydrazide and hippuric acid ivas about 4. Twenty-six new diacylhydrazines were prepared. In the reaction between DL-mandelic hydrazide and hippuric acid no resolution occurred, but a racemic product resulted. An attempted partial asymmetric synthesis in the reaction between ethylmalonic hydrazide and carbobenzoxyglycine was not successful, but this reaction likewise gave a racemic product.

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Amino Acid Derivatives. II. Enzymatic Synthesis of Phenylhydrazides of Carboallyloxyamino Acids^1,2

Cited by 13 publications

References 0 publications

α-Chymotrypsin as the catalyst for peptide synthesis

α-Chymotrypsin as the catalyst for peptide synthesis

The Synthesis of α-Methyltryptophans and α-Alkyltryptamines

Resolutions and an Attempted Partial Asymmetric Synthesis in Papain-Catalyzed Syntheses of N^α,N^β-Diacylhydrazines from Hydrazides and Acylated Amino Acids

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Amino Acid Derivatives. II. Enzymatic Synthesis of Phenylhydrazides of Carboallyloxyamino Acids1,2

Cited by 13 publications

References 0 publications

α-Chymotrypsin as the catalyst for peptide synthesis

α-Chymotrypsin as the catalyst for peptide synthesis

The Synthesis of α-Methyltryptophans and α-Alkyltryptamines

Resolutions and an Attempted Partial Asymmetric Synthesis in Papain-Catalyzed Syntheses of Nα,Nβ-Diacylhydrazines from Hydrazides and Acylated Amino Acids

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Amino Acid Derivatives. II. Enzymatic Synthesis of Phenylhydrazides of Carboallyloxyamino Acids^1,2

Resolutions and an Attempted Partial Asymmetric Synthesis in Papain-Catalyzed Syntheses of N^α,N^β-Diacylhydrazines from Hydrazides and Acylated Amino Acids