Classification and Nomenclature of Enzymes
... • EC numbers are four digits, for example a.b.c.d, where “a” is the class, “b” is the subclass, “c” is the sub‐subclass, and “d” is the sub‐sub‐subclass. The “b” and “c” digits describe the reaction, while the “d” digit is used to distinguish between different enzymes of the same function based ...
... • EC numbers are four digits, for example a.b.c.d, where “a” is the class, “b” is the subclass, “c” is the sub‐subclass, and “d” is the sub‐sub‐subclass. The “b” and “c” digits describe the reaction, while the “d” digit is used to distinguish between different enzymes of the same function based ...
Previous lecture: Today:
... •Uncatalyzed reactions, even when thermodynamically favorable (spontaneous), often are extremely slow. •They are slow because of the height of the activation energy needed to reach the transition state •Activation energy is high because the formation of the transition state is unfavorable due to the ...
... •Uncatalyzed reactions, even when thermodynamically favorable (spontaneous), often are extremely slow. •They are slow because of the height of the activation energy needed to reach the transition state •Activation energy is high because the formation of the transition state is unfavorable due to the ...
Chapter 6
... In an enzyme, functional groups in the active site can perform the same catalytic faction as in chemical reactions such as acid/base reactions, transient covalent bonds and charge-charge interactions. Functional groups cannot do redox reactions or group transfer reactions. For those you need a bound ...
... In an enzyme, functional groups in the active site can perform the same catalytic faction as in chemical reactions such as acid/base reactions, transient covalent bonds and charge-charge interactions. Functional groups cannot do redox reactions or group transfer reactions. For those you need a bound ...
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034
... (6) Only the amino acids present at the active site of an enzyme are involved in product formation. (7) Replacement of the glutamate at the 35th position in lysozyme with serine would Inactivate lysozyme. (8) Introduction of proline residues at specific positions in an enzyme structure improves its ...
... (6) Only the amino acids present at the active site of an enzyme are involved in product formation. (7) Replacement of the glutamate at the 35th position in lysozyme with serine would Inactivate lysozyme. (8) Introduction of proline residues at specific positions in an enzyme structure improves its ...
Amino Acids and the Primary Structure of Proteins
... Cleaving Disulfide bonds and Protecting the thiols formed • Disulfide bonds in proteins must be cleaved: (1) To permit isolation of the PTH-cysteine during the Edman procedure (2) To separate peptide chains • Treatment with thiol compounds reduces the (R-S-S-R) cystine bond to two cysteine (R-SH) r ...
... Cleaving Disulfide bonds and Protecting the thiols formed • Disulfide bonds in proteins must be cleaved: (1) To permit isolation of the PTH-cysteine during the Edman procedure (2) To separate peptide chains • Treatment with thiol compounds reduces the (R-S-S-R) cystine bond to two cysteine (R-SH) r ...
ENZYMOLOGY
... Lipoic acid is a cofactor of the multienzyme complexes pyruvic dehydrogenase (PDH) and αketoglutaric dehydrogenase (α-KDH). There is no evidence of a requirement by man who presumably can synthesize it in the amounts required. Lipoic acid exists in both oxidized and reduced forms due to the ability ...
... Lipoic acid is a cofactor of the multienzyme complexes pyruvic dehydrogenase (PDH) and αketoglutaric dehydrogenase (α-KDH). There is no evidence of a requirement by man who presumably can synthesize it in the amounts required. Lipoic acid exists in both oxidized and reduced forms due to the ability ...
Syllabus Notes - Southwest High School
... Mono: mainly used as an energy source. Remember! A mono has 6 or fewer ‘C’ and equal ‘O’! Glucose is C6H12O6. Polysaccharides are energy storage (glycogen and starch) or STRUCTURE (cellulose = ...
... Mono: mainly used as an energy source. Remember! A mono has 6 or fewer ‘C’ and equal ‘O’! Glucose is C6H12O6. Polysaccharides are energy storage (glycogen and starch) or STRUCTURE (cellulose = ...
Gene Section TMPRSS2 (transmembrane protease, serine 2) Atlas of Genetics and Cytogenetics
... © 2010 Atlas of Genetics and Cytogenetics in Oncology and Haematology ...
... © 2010 Atlas of Genetics and Cytogenetics in Oncology and Haematology ...
Enzymes - Westgate Mennonite Collegiate
... - high temps may denature (unfold) the enzyme. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions) ...
... - high temps may denature (unfold) the enzyme. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions) ...
Enzymes
... What would happen if you boil it? Guesses -____denature________ What would happen if you put it in acid? _______denature_________ What would happen in the cold?________inhibit________ ...
... What would happen if you boil it? Guesses -____denature________ What would happen if you put it in acid? _______denature_________ What would happen in the cold?________inhibit________ ...
Enzymes lecture 2
... Inhibitors: Thiol blocking compounds, heavy metal ions, histidine, and certain amines. Tris should not be used as a buffer due to its inhibitory effect. Storage: Store at 2-8° C. ...
... Inhibitors: Thiol blocking compounds, heavy metal ions, histidine, and certain amines. Tris should not be used as a buffer due to its inhibitory effect. Storage: Store at 2-8° C. ...
Physical Properties - Winthrop University
... 1. Nucleophilic Substitution Reactions: An electron rich atom (nucleophile) attacks a electron deficient atom 2. Acid-Base Catalysis: Certain amino acid side chains of enzymes can accept or donate protons, making them act like acids (donate protons) or bases (accept protons) 3. Condensation Reaction ...
... 1. Nucleophilic Substitution Reactions: An electron rich atom (nucleophile) attacks a electron deficient atom 2. Acid-Base Catalysis: Certain amino acid side chains of enzymes can accept or donate protons, making them act like acids (donate protons) or bases (accept protons) 3. Condensation Reaction ...
Keratin
... • A planar peptide bond reduced the number of conformations of a poly-peptide chain and led to their proposal of the alpha helix and the beta sheet. • alpha-helix explained the x-ray data which showed a repeat unit of 0.50 – 0.55 nm. This distance corresponds to the height of the rise per revolution ...
... • A planar peptide bond reduced the number of conformations of a poly-peptide chain and led to their proposal of the alpha helix and the beta sheet. • alpha-helix explained the x-ray data which showed a repeat unit of 0.50 – 0.55 nm. This distance corresponds to the height of the rise per revolution ...
Organic vs. Inorganic
... (chemical reactions) in the body. •Weaken chemical bonds so molecules can be made or broken down by the body •Many end is ~ase ...
... (chemical reactions) in the body. •Weaken chemical bonds so molecules can be made or broken down by the body •Many end is ~ase ...
Catalytic triad
A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.