No Slide Title
... Chymotrypsin, trypsin and elastase are examples of the major class of proteases known as serine proteases (discussed in lecture 15) which are so named because they have a highly reactive serine at the active site that is essential for catalytic activity. Different members of the serine protease fam ...
... Chymotrypsin, trypsin and elastase are examples of the major class of proteases known as serine proteases (discussed in lecture 15) which are so named because they have a highly reactive serine at the active site that is essential for catalytic activity. Different members of the serine protease fam ...
Answers for extension worksheet – Option C
... If an organism is starving, protein can be used as a source of energy. Protein is split into amino acids, which are then deaminated (the NH2 group is removed). The remainder of the molecule enters the respiratory process. Some amino acids are converted to pyruvate, others enter the Krebs cycle. In e ...
... If an organism is starving, protein can be used as a source of energy. Protein is split into amino acids, which are then deaminated (the NH2 group is removed). The remainder of the molecule enters the respiratory process. Some amino acids are converted to pyruvate, others enter the Krebs cycle. In e ...
Enzyme Kinetics
... – Given a reaction (including names) – Use subclass designation if appropriate ...
... – Given a reaction (including names) – Use subclass designation if appropriate ...
Enzymes - NVHSIntroBioPiper1
... catalysts to speed up chemical reactions Identify many enzymes by the suffix ...
... catalysts to speed up chemical reactions Identify many enzymes by the suffix ...
CO-ENZYMES i.
... 5. The active site is contributed by amino acid residues that are far apart in the enzyme molecule. During catalysis, they are brought together. 6. The amino acids at the active site are arranged in a very precise manner so that only specific substrate can bind at the active site. 7. Usually serine, ...
... 5. The active site is contributed by amino acid residues that are far apart in the enzyme molecule. During catalysis, they are brought together. 6. The amino acids at the active site are arranged in a very precise manner so that only specific substrate can bind at the active site. 7. Usually serine, ...
Option B IB Chemistry Definitions HL
... (product from the citric acid cycle) move along cytochromes by repeated redox reactions, due to presence of stronger oxidizing agents. Enzyme cytochrome oxidase causes H+ ions, e- and O2 to react to form water, releasing energy in the process. ...
... (product from the citric acid cycle) move along cytochromes by repeated redox reactions, due to presence of stronger oxidizing agents. Enzyme cytochrome oxidase causes H+ ions, e- and O2 to react to form water, releasing energy in the process. ...
Biochem PowerPoint Presentation
... - Substrate molecule fits in shape of active site - Active sites are specific for substrates ...
... - Substrate molecule fits in shape of active site - Active sites are specific for substrates ...
An Investigation into the Minimum Requirements for
... 1.7 X lod “The error in these determinations was 10-20%. The buffers were 100 mM NaC1/2O mM CaCI, and either 50 mM Tris-C1, pH 8.0, or 50 mM glycine, pH 10.1. Similar results were observed at pH 8.0 with 50 mM MOPS. The experiments were allowed to proceed until more than one turnover had occurred. T ...
... 1.7 X lod “The error in these determinations was 10-20%. The buffers were 100 mM NaC1/2O mM CaCI, and either 50 mM Tris-C1, pH 8.0, or 50 mM glycine, pH 10.1. Similar results were observed at pH 8.0 with 50 mM MOPS. The experiments were allowed to proceed until more than one turnover had occurred. T ...
Biology I SB1bc Enzymes and Macromolecules Test Study Guide
... “Reusable” proteins that put together or break down substrates to form products 2. Since enzymes are proteins they are made of ……what? Amino acids joined by peptide bonds 3. The energy needed to start a chemical reaction is called? Activation Energy (EA) 4. How do enzymes increase the rate or speed ...
... “Reusable” proteins that put together or break down substrates to form products 2. Since enzymes are proteins they are made of ……what? Amino acids joined by peptide bonds 3. The energy needed to start a chemical reaction is called? Activation Energy (EA) 4. How do enzymes increase the rate or speed ...
Biosynthesis of the nutritionally nonessential amino acids
... 1. Glutamine: This amino acid, which contains an amide linkage with ammonia at the γ-carboxyl, is formed from glutamate by glutamine synthetase The reaction is driven by the hydrolysis of ATP. This reaction also serves as a major mechanism for the detoxification of ammonia in brain and liver . 2. As ...
... 1. Glutamine: This amino acid, which contains an amide linkage with ammonia at the γ-carboxyl, is formed from glutamate by glutamine synthetase The reaction is driven by the hydrolysis of ATP. This reaction also serves as a major mechanism for the detoxification of ammonia in brain and liver . 2. As ...
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 = ...
Enzyme specificity
... Enzymes are Specific Remember: Enzymes are specific because of their shape. ...
... Enzymes are Specific Remember: Enzymes are specific because of their shape. ...
Exam 1
... 19. If a -sandwich motif is found on the surface of a protein, it must be ___________________________ so that one face can interact with the water favorably while the other face forms favorable interactions with the core of the protein. 20. _____________________ is a nucleobase found in RNA but not ...
... 19. If a -sandwich motif is found on the surface of a protein, it must be ___________________________ so that one face can interact with the water favorably while the other face forms favorable interactions with the core of the protein. 20. _____________________ is a nucleobase found in RNA but not ...
Questions
... 2. Based on results described in question 1, investigators used the technique of sitedirected mutagenesis to synthesize five mutant CK proteins in which the Cys278 residue was replaced with either a Gly, Ser, Ala , Asn or Asp residue. The mutants were called C278G, C278S, C278A, C278N and C278D, re ...
... 2. Based on results described in question 1, investigators used the technique of sitedirected mutagenesis to synthesize five mutant CK proteins in which the Cys278 residue was replaced with either a Gly, Ser, Ala , Asn or Asp residue. The mutants were called C278G, C278S, C278A, C278N and C278D, re ...
ch3a FA11 - Cal State LA
... How to lower EA • Mechanism: form an Enzyme-Substrate (ES) complex at active site – Enhance substrate reactivity • Enhance polarity of bonds via interaction with amino acid functional groups • Possibly form covalent bonded intermediates with amino acid side chains ...
... How to lower EA • Mechanism: form an Enzyme-Substrate (ES) complex at active site – Enhance substrate reactivity • Enhance polarity of bonds via interaction with amino acid functional groups • Possibly form covalent bonded intermediates with amino acid side chains ...
Chapter 4
... Transferases – transfer a functional group Hydrolases – hydrolytic cleavage Proteases – hydrolytic cleavage of protein chains Kinases – add phosphate groups to compounds … and many, many more… ...
... Transferases – transfer a functional group Hydrolases – hydrolytic cleavage Proteases – hydrolytic cleavage of protein chains Kinases – add phosphate groups to compounds … and many, many more… ...
Enzymes
... orientation for the reaction. As the active site binds the substrate, it may put stress on bonds that must be broken, making it easier to reach the transition state. R groups at the active site may create a conducive microenvironment for a specific reaction. Enzymes may even bind covalently to subst ...
... orientation for the reaction. As the active site binds the substrate, it may put stress on bonds that must be broken, making it easier to reach the transition state. R groups at the active site may create a conducive microenvironment for a specific reaction. Enzymes may even bind covalently to subst ...
Structural Biochemistry/Enzyme Regulation
... substrate T can bind and react with the newly modified active site. Once the newly formed product leaves the enzyme it returns to its original state ready to accept substrate S. Enzymes that exhibit this mechanism include thioredoxin peroxidase, cytydilytransferase, and chymotrypsin. Serine protease ...
... substrate T can bind and react with the newly modified active site. Once the newly formed product leaves the enzyme it returns to its original state ready to accept substrate S. Enzymes that exhibit this mechanism include thioredoxin peroxidase, cytydilytransferase, and chymotrypsin. Serine protease ...
Unconventional serine proteases: Variations on the catalytic Ser/His
... Chymotrypsin numbering is conventionally used for sequence and structure comparisons within clan PA such that the catalytic nucleophile is Ser195, the general base is His57, and the aspartate residue is Asp102 (Fig. 2). The backbone amide nitrogens of Gly193 and Ser195 form the oxyanion hole. The se ...
... Chymotrypsin numbering is conventionally used for sequence and structure comparisons within clan PA such that the catalytic nucleophile is Ser195, the general base is His57, and the aspartate residue is Asp102 (Fig. 2). The backbone amide nitrogens of Gly193 and Ser195 form the oxyanion hole. The se ...
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.