Below is the process diagram of lysozyme reaction mechanism. Please help me brea

Question

Below is the process diagram of lysozyme reaction mechanism.

Please help me break down/simplify the diagram to cleary illustrate the transition state showing chair to coplanar form in order to answer the following question:

Draw mechanism of reaction of lysozyme to illustrate ONLY the general covalent catalysis.

HOCH2 OR' H HOCH Water binding CH2 CH2 Glu35 CH2 -CH2- Glu35 Substrate HOCH2 HOCH2 polysaccharide OR' H Binding CH. Asp52 CH Asp52 HOCH2 General acid General base catalysis catalysis HONOH H CH2 CH Glu35 CH CH Glu35 HOCH HOCH OR H OR H M oxonium ion (transition state) CH Asp52 CH2 Asp52 CH2 CH. Glu35 HOCH Covalent catalysis OR H H20 CH2 Asp52 Covalent intermediate

Explanation / Answer

Covalent Catalysis one of the four strategies that an enzyme will employ to catalyze a specific reaction. In this reaction the enzyme contains a reactive group, usually a nucleophilic residue which reacts with the substrate through a nucleophilic attack. The residue becomes covalently attached to the substrate throughout the catalytic reaction adding an additional intermediate which helps stabilize later transition states by lowering the activation energy. The covalent bond is then broken to regenerate enzymes.

In the above lysozyme reaction the glutamic portion of enzyme (glu35) first break the glycosidic linkages between monomers of polysaccharides which produce a monomers with a carbon having postive charge. Now the aspartic portion of lysozyme (act as nucleophile since it has negative charge) attacks on the positive charge (nucleophilic attack) which creats a covalent bond between monomers and enzymes. This covalent bond further hydrolysed to make free the lysozyme. Since covalent bond formation takes place, this step is known as covalent catalysis.

Related Questions

Navigate

• Browse (All)
• Browse B
• Subjects

---

---

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.