Kinetics and Equilibrium for Thermolysin-Catalyzed Syntheses of Dipeptide Precursors in Aqueous/Organic Biphasic Systems.

Miyanaga, Masamitsu; Ohmori, Manabu; IMAMURA, KOREYOSHI; Sakiyama, Takaharu; NAKANISHI, KAZUHIRO

doi:10.1263/jbb.90.43

Cited by 4 publications

(7 citation statements)

References 9 publications

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“…Capsaicin derivatives were synthesized in an aqueous/organic biphasic system that permits the equilibrium of reaction to be shifted toward synthesis (8,9). n-Hexane was selected as the organic solvent for the reaction.…”

Section: Resultsmentioning

confidence: 99%

“…One approach to this would be to synthesize capsaicin analogues from vanillylamine and fatty acids using the reverse reaction of hydrolysis, using a capsaicin-hydrolyzing enzyme in an organic solvent, similar to the procedures used to prepare peptide precursors using proteases (8,9). We report herein on the purification/characterization of a novel acylase from Streptomyces mobaraensis NBRC (IFO) 13819 that principally catalyzes the hydrolysis of capsaicin and synthesis of capsaicin derivatives.…”

Section: Introductionmentioning

confidence: 99%

“…NR-Lauroyl-dipeptides were synthesized from 100 mM dipeptides and 7.5 mM lauric acid in buffer E with 78% glycerol (O) and without glycerol (0). N -Lauroyl-dipeptides were synthesized in buffer E with 78% glycerol (b) and without glycerol(9).…”

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confidence: 99%

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A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

Koreishi

Zhang

Imanaka

et al. 2005

J. Agric. Food Chem.

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A novel enzyme that catalyzes efficient hydrolysis of capsaicin (8-methyl-N-vanillyl-6-nonenamide) was isolated from the culture broth of Streptomyces mobaraensis. The enzyme consisted of two dissimilar subunits with molecular masses of 61 and 19 kDa. The enzyme was activated and stabilized in the presence of Co2+. It showed a pH optimum of about 8 and was stable at temperatures of up to 55 degrees C for 1 h at pH 7.8. The specific activity of the enzyme for the hydrolysis of capsaicin was 10(2)-10(4) times higher than those for the enzymes reported to date. In an aqueous/n-hexane biphasic system, capsaicin analogues such as octanoyl, decanoyl, and lauroyl vanillylamides were synthesized from the corresponding fatty acids and vanillylamine at yields of 50% or greater. In addition, the enzyme catalyzed the deacylation of N-lauroyl-L-amino acids and N-lauroyl-L-dipeptides and the efficient synthesis of Nalpha-lauroyl-L-lysine, Nepsilon-lauroyl-L-lysine, and various N-lauroyl-peptides in aqueous solution in both the absence and the presence of glycerol.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

Koreishi

Zhang

Imanaka

et al. 2005

J. Agric. Food Chem.

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“…In order to further assess the utility of 1, 4-8c as acyl donor probes, we also screened their reactivity with CLEC-thermolysin (TL-CLEC) 20 as a protease with a different substrate specificity profile, that includes b-aspartate esters. 21 However, TL-CLEC also failed to accept 4-8c and again only 1c was accepted, allowing the preparation of 16b from 16a in 48% yield.…”

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confidence: 99%

“…Carbohydrate-amino acid coupling reactions 2 mg ml21 of lyophilized (from pH 8.0, 0.1 M phosphate) SBL preparation, 45 °C, anhydrous pyridine, 120 h. b 1 mg ml 21 of TL-CLEC, 45 °C, 1+25 water-pyridine. c All yields are for isolated, purified, single compounds.…”

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Ready protease-catalyzed synthesis of carbohydrate–amino acid conjugates

et al. 2001

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The protease-catalyzed synthesis of amino acid est-carbohydrate conjugates as glycopeptide analogues has been achieved in a highly regioselective and carbohydrate-specific manner using amino acid vinyl ester acyl donors and minimally or completely unprotected carbohydrate acyl acceptors, which together probed active sites of proteases to reveal yield efficiencies that are modulated by the carbohydrate C-2 substitutent, and that may be exploited to allow selective one-pot syntheses.

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