Hydrolysis and Synthesis of Peptides

Nuijens, Timo; Quaedflieg, Peter J. L. M.; Jakubke, Hans‐Dieter

doi:10.1002/9783527639861.ch17

Cited by 7 publications

(6 citation statements)

References 229 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzymatic catalysis can be regulated by the characteristics of the enzymes. Generally, proteases are known for their hydrolysis efficiency, but they can also function in the opposite direction, leading to the formation of peptide bonds (aminolysis) [1,10]. Hydrolysis and aminolysis often compete with each other.…”

Section: Reaction Mechanismsmentioning

confidence: 99%

“…The major drawbacks of the equilibrium-controlled synthesis include low yield and a slow reaction rate as compared to the kinetically controlled reactions. Larger quantities of the enzyme are also needed [1]. Optimal reaction conditions are required for directing the reaction toward peptide synthesis.…”

Section: Reaction Mechanismsmentioning

confidence: 99%

“…The reaction substrate decreases gradually during the course of the reaction, and the effect of hydrolysis increases. It is therefore important to stop the aminolysis reaction before the rate of hydrolysis exceeds the rate of aminolysis [1]. The success of the aminolysis reaction depends on the aminolysis:hydrolysis ratio, which is determined by many factors such as enzyme specificity and substrate concentration, as well as the presence of activated carboxyl groups.…”

Section: Reaction Mechanismsmentioning

confidence: 99%

“…Linear and circular peptides play important roles in biological reactions and are therefore considered important target molecules for pharmaceutical, nutritional, and cosmetic applications [1]. Peptides are formed when the amino group of one amino acid forms an amide (peptide) linkage with the carboxyl group of another amino acid.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Recent Advances in Chemoenzymatic Peptide Syntheses

Yazawa

Numata

2014

Molecules

View full text Add to dashboard Cite

Chemoenzymatic peptide synthesis is the hydrolase-catalyzed stereoselective formation of peptide bonds. It is a clean and mild procedure, unlike conventional chemical synthesis, which involves complicated and laborious protection-deprotection procedures and harsh reaction conditions. The chemoenzymatic approach has been utilized for several decades because determining the optimal conditions for conventional synthesis is often time-consuming. The synthesis of poly-and oligopeptides comprising various amino acids longer than a dipeptide continues to pose a challenge owing to the lack of knowledge about enzymatic mechanisms and owing to difficulty in optimizing the pH, temperature, and other reaction conditions. These drawbacks limit the applications of the chemoenzymatic approach. Recently, a variety of enzymes and substrates produced using recombinant techniques, substrate mimetics, and optimal reaction conditions (e.g., frozen aqueous media and ionic liquids) have broadened the scope of chemoenzymatic peptide syntheses. In this review, we highlight the recent advances in the chemoenzymatic syntheses of various peptides and their use in developing new materials and biomedical applications.

show abstract

Section: Reaction Mechanismsmentioning

confidence: 99%

Section: Reaction Mechanismsmentioning

confidence: 99%

Section: Reaction Mechanismsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Recent Advances in Chemoenzymatic Peptide Syntheses

Yazawa

Numata

2014

Molecules

View full text Add to dashboard Cite

show abstract

“…The use of native Trypsin and engineered variants for peptide synthesis has been known for decades (Nuijens et al, 2012). Recently, Bordusa et al discovered a new engineered Trypsin variant, termed Trypsiligase, which can be used for the N- and C- terminal modification of protein or peptide substrates (Liebscher et al, 2014b).…”

Section: Trypsin Related Enzymesmentioning

confidence: 99%

Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization

et al. 2019

Self Cite

View full text Add to dashboard Cite

The renaissance of peptides as prospective therapeutics has fostered the development of novel strategies for their synthesis and modification. In this context, besides the development of new chemical peptide ligation approaches, especially the use of enzymes as a versatile tool has gained increased attention. Nowadays, due to their inherent properties such as excellent regio- and chemoselectivity, enzymes represent invaluable instruments in both academic and industrial laboratories. This mini-review focuses on natural- and engineered peptide ligases that can form a new peptide (amide) bond between the C-terminal carboxy and N-terminal amino group of a peptide and/or protein. The pro's and cons of several enzyme classes such as Sortases, Asparaginyl Endoproteases, Trypsin related enzymes and as a central focus subtilisin-derived variants are summarized. Most recent developments with regards to ligation and cyclization are highlighted.

show abstract

Racemizable Acyl Donors for Enzymatic Dynamic Kinetic Resolution

Tessaro

2014

Cascade Biocatalysis

View full text Add to dashboard Cite

Hydrolysis and Synthesis of Peptides

Cited by 7 publications

References 229 publications

Recent Advances in Chemoenzymatic Peptide Syntheses

Recent Advances in Chemoenzymatic Peptide Syntheses

Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization

Racemizable Acyl Donors for Enzymatic Dynamic Kinetic Resolution

Contact Info

Product

Resources

About