Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Jakubke, Hans‐Dieter; Kuhl, P.; Könnecke, Andreas

doi:10.1002/ange.19850970204

Cited by 71 publications

(24 citation statements)

References 54 publications

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“…They show that the formation of alkyl fructosides is dependent on enzyme concentration. It decreases as the enzyme concentration increases, whereas the conversion rate of sucrose increases and attains 100% at 24 U/mL after 8 h. Therefore, in addition to reactions (1) and ( 2 ) , with reaction ( 3 ) , the cleavage of alkyl fructosides occurs. At high enzyme concentrations, all three reactions are accelerated until, finally, complete conversion of both sucrose and alkyl fructoside is obtained.…”

Section: Formation Of Alkyl Fructosides From Sucrosementioning

confidence: 91%

Invertase‐catalyzed reactions in alcoholic solutions

Selisko

Ulbrich

Schellenberger

et al. 1990

Biotech & Bioengineering

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The formation of alkyl beta-D-fructofuranosides by invertase from sucrose in aqueous solutions of methanol, ethanol, or n-propanol is studied for the dependence on alcohol and invertase concentrations as well as on reaction time. The yield of alkyl beta-D-fructosides is shown to be controlled by three competitive reactions: the alcoholysis of sucrose, the hydrolysis of sucrose, and the hydrolysis of alkyl beta-D-fructosides. Both the conversion rate of sucrose and the fraction of alkyl beta-D-fructosides in the product mixture are dependent on the chain length of the alcohols. They decrease in the sequence methanol > ethanol > n-propanol. Alkyl beta-D-fructosides are also formed by invertase starting from alcoholic solutions of fructose.

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Section: Formation Of Alkyl Fructosides From Sucrosementioning

confidence: 91%

Invertase‐catalyzed reactions in alcoholic solutions

Selisko

Ulbrich

Schellenberger

et al. 1990

Biotech & Bioengineering

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“…[16,17,19] This can be achieved by increasing the pH of the reaction medium. However, a pH> 8 generally results in w-laurolactam hydrolase deactivation.…”

Section: Laurolactam Synthesis From 12-aminododecanoic Acidmentioning

confidence: 99%

Enzyme‐Catalyzed Laurolactam Synthesis via Intramolecular Amide Bond Formation in Aqueous Solution

et al. 2011

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Lactam formation from w-aminocarboxylic acids is thermodynamically unfavored in aqueous solution and therefore hard to achieve. In the present work w-laurolactam hydrolases from Acidovorax sp. T31 and Cupriavidus sp. U124 were investigated regarding their potential to catalyze lactam formation. Both enzymes are known to hydrolyze laurolactam to 12-aminododecanoic acid. The w-laurolactam hydrolase genes were expressed in Escherichia coli BL21 (DE3) and the catalytic activity of the respective proteins was investigated. As expected from thermodynamics, only laurolactam hydrolysis but not 12-aminododecanoic acid cyclization was observed in whole-cell biotransformations and cell extract assays. The utilization of 12-aminododecanoic acid methyl ester, as an activated form of 12-aminododecanoic acid, resulted in intramolecular amide bond formation with the product laurolactam. Maximum laurolactam formation rates of 13.5 and 14.3 U g CDW À1 and molar yields of 11.5% and 13.0% were achieved in biotransformations at pH 10 with recombinant E. coli harboring the w-laurolactam hydrolase from Cupriavidus sp. U124 and Acidovorax sp. T31, respectively. Furthermore, it was shown that under the harsh reaction conditions applied, the utilization of whole-cell biocatalysts enables 17.2-fold higher laurolactam formation activity in comparison to free enzymes in solution. This study shows that hydrolasecatalyzed laurolactam synthesis can be achieved in aqueous solution by selection of an appropriate substrate and reaction pH.

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“…Diese Barriere wird durch den Transfer eines Protons vom nucleophilen Amin auf das elektrophile Carboxylat repräsentiert. [263,265] Durch Zusatz organischer Lösungsmittel zum Reaktionsansatz kann die Dielektrizitätskonstante des Mediums und damit die Azidität der Carboxylgruppe gesenkt werden. Infolgedessen sind Proteasen in organischen oder wässrigen Lösungsmitteln zur Katalyse von Peptidkupplungen fähig, jedoch ist es meist erforderlich, optimierte Reaktionsbedingungen sowie eigens modifizierte Proteasen zu verwenden.…”

Section: Reverse Proteolyseunclassified

Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine

2008

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Die Untersuchung biologischer Fragestellungen mit chemischen Methoden wird meist als “Chemische Biologie” bezeichnet und setzt voraus, dass biologisch relevante Makromoleküle, wie Peptide und Proteine, chemisch zugänglich sind. Auf der Festphasensynthese von Peptiden aufbauend wurden viele chemoselektive Ligations‐ und Modifikationstechniken zur Verknüpfung synthetischer Peptide oder funktionaler Einheiten zu größeren synthetischen, biologisch relevanten Makromolekülen entwickelt. Dieser Aufsatz fasst die aktuellen Entwicklungen auf dem Gebiet der chemoselektiven Ligations‐ und Modifikationsstrategien zusammen und illustriert ihre Anwendbarkeit an Beispielen aus der chemischen Totalsynthese von Proteinen bis hin zur Semisynthese natürlicher modifizierter Proteine.

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Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Cited by 71 publications

References 54 publications

Invertase‐catalyzed reactions in alcoholic solutions

Invertase‐catalyzed reactions in alcoholic solutions

Enzyme‐Catalyzed Laurolactam Synthesis via Intramolecular Amide Bond Formation in Aqueous Solution

Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine

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