Chymotrypsin - Catalysis

What is Chymotrypsin?

Chymotrypsin is a serine protease enzyme that plays a crucial role in the digestive system by breaking down proteins into smaller peptides. It is synthesized in the pancreas as an inactive precursor, chymotrypsinogen, and activated in the small intestine.

How Does Chymotrypsin Catalyze Reactions?

Chymotrypsin catalyzes the hydrolysis of peptide bonds. It employs a catalytic triad consisting of serine, histidine, and aspartate residues. The mechanism involves a nucleophilic attack by the serine residue on the carbonyl carbon of the peptide bond, forming a tetrahedral intermediate. This intermediate is stabilized by a structure known as the oxyanion hole, facilitating the breakdown of the peptide bond.

What is the Specificity of Chymotrypsin?

Chymotrypsin exhibits specificity for peptide bonds adjacent to aromatic amino acids such as tryptophan, tyrosine, and phenylalanine. This specificity is attributed to its hydrophobic pocket, which accommodates the aromatic side chains of these amino acids.

What are the Kinetic Properties of Chymotrypsin?

The catalytic efficiency of chymotrypsin can be described by the Michaelis-Menten equation. Key parameters include the Michaelis constant (Km) and the catalytic turnover number (kcat). These values provide insight into the enzyme's affinity for substrates and its maximum catalytic rate.

How is Chymotrypsin Regulated?

Chymotrypsin activity is regulated through several mechanisms. It is initially produced as an inactive zymogen to prevent premature activity. Activation is mediated by the proteolytic cleavage of chymotrypsinogen by trypsin. Additionally, enzyme inhibitors such as serpins can modulate its activity to prevent uncontrolled proteolysis.

What are the Industrial and Medical Applications of Chymotrypsin?

Chymotrypsin has significant applications in both industrial and medical fields. It is used in the production of protein hydrolysates and in the leather industry to remove hair from hides. Medically, chymotrypsin is employed as an anti-inflammatory agent and in the treatment of conditions such as cystic fibrosis to digest thick mucus.

Why is Chymotrypsin Important in Catalysis Research?

Chymotrypsin serves as a model enzyme in the study of enzyme kinetics and catalysis. Its well-characterized mechanism provides a framework for understanding the principles of enzymatic catalysis and for designing enzyme inhibitors and other therapeutic agents. Insights gained from studying chymotrypsin have broad implications for biochemistry and molecular biology.

Relevant Publications

Novel chymotrypsin C (CTRC) variants from real-world genetic testing of pediatric chronic pancreatitis cases.

Issue Release: 2024

Dietary vitamin C reduces mortality of Pacific white shrimp (Penaeus vannamei) post-larvae by Vibrio parahaemolyticus challenge.

Issue Release: 2024

Design and synthesis of a nucleobase functionalized peptide hydrogel: assessment of anti-inflammatory and wound healing effects.

Issue Release: 2024

3-Chymotrypsin-like Protease (3CLpro) of SARS-CoV-2: Validation as a Molecular Target, Proposal of a Novel Catalytic Mechanism, and Inhibitors in Preclinical and Clinical Trials.

Issue Release: 2024

Revealing the interaction between alpha-chymotrypsin and eugenol: An integrated multi-spectral and dynamic simulation approach.

Issue Release: 2024

Bowman-Birk Inhibitor Mutants of Soybean Generated by CRISPR-Cas9 Reveal Drastic Reductions in Trypsin and Chymotrypsin Inhibitor Activities.

Issue Release: 2024

Targeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability.

Issue Release: 2024

Cottonseed meal protein hydrolysate influences growth performance, carcass characteristics, serum biochemical indices, and intestinal morphology in yellow-feather broilers.

Issue Release: 2024

[Effects of removing superficial layer of cartilage on the surface morphology and mechanical behavior of cartilage].

Issue Release: 2024

Cellulose acetate microwell plates for high-throughput colorimetric assays.

Issue Release: 2024

Modular and integrative activity reporters enhance biochemical studies in the yeast ER.

Issue Release: 2024

Predicting drug-Protein interaction with deep learning framework for molecular graphs and sequences: Potential candidates against SAR-CoV-2.

Issue Release: 2024

Onnamide A suppresses the severe acute respiratory syndrome-coronavirus 2 infection without inhibiting 3-chymotrypsin-like cysteine protease.

Issue Release: 2024

Maintenance of an Acidic Skin Surface with a Novel Zinc Lactobionate Emollient Preparation Improves Skin Barrier Function in Patients with Atopic Dermatitis.

Issue Release: 2024

Chymotrypsin and Trypsin Inhibitory Activity of Some Medicinal Plants Collected from Rize (Türkiye).

Issue Release: 2024

Repurposing proteasome inhibitors for improved treatment of triple-negative breast cancer.

Issue Release: 2024

Application of a crude digestive proteases preparation to improve the ripening of marinated fillets from low-technological value Baltic herring (Clupea harengus membras L.).

Issue Release: 2024

Isolation and structure determination of a new depsipeptide crocapeptin C from the myxobacterium .

Issue Release: 2024

A Multicomponent Mannich Reaction Catalyzed by Hydrolases Immobilized on Titanate Nanotubes.

Issue Release: 2024

Development of a GC-376 Based Peptidomimetic PROTAC as a Degrader of 3-Chymotrypsin-like Protease of SARS-CoV-2.

Issue Release: 2024

What is an Inventive Step?

What Are the Safety Considerations?

What are the Benefits for Catalyst Suppliers?

What are Histone Acetyltransferases?

What are the Strategies to Prevent Catalyst Melting?

What is a Digital Twin?

Why Use CFD in Catalysis?

What Precautions Should Be Taken During Catalysis Experiments?

What are the Benefits of Regular Audits?

How is Surface Reconstruction Studied?

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