Chapter 6. Metabolism & Enzymes
... Induced fit model More accurate model of enzyme action 3-D structure of enzyme fits substrate as substrate binds, enzyme changes shape leading to a tighter fit ...
... Induced fit model More accurate model of enzyme action 3-D structure of enzyme fits substrate as substrate binds, enzyme changes shape leading to a tighter fit ...
Polar amino acids with negative charge
... Cysteine differs from serine in a single atom-- the sulfur of the thiol replaces the oxygen of the alcohol. The amino acids are, however, much more different in their physical and chemical properties than their similarity might suggest. Cysteine also plays a key role in stabilizing extracellular pro ...
... Cysteine differs from serine in a single atom-- the sulfur of the thiol replaces the oxygen of the alcohol. The amino acids are, however, much more different in their physical and chemical properties than their similarity might suggest. Cysteine also plays a key role in stabilizing extracellular pro ...
MOLECULAR BIOCHEMISTRY II INTRODUCTORY LECTURE
... Linus Pauling in “The Nature of the Chemical Bond” ...
... Linus Pauling in “The Nature of the Chemical Bond” ...
The Kinetics of Enzyme Catalyzed Reactions
... Most synthetic catalyst are not specific i.e., they will catalyze similar reactions involving many different kinds of reactants. While enzymes are specific. They will catalyze only one reaction involving only certain substances. ...
... Most synthetic catalyst are not specific i.e., they will catalyze similar reactions involving many different kinds of reactants. While enzymes are specific. They will catalyze only one reaction involving only certain substances. ...
cOmplete, Mini, EDTA-free - Sigma
... metal affinity chromatography) cOmplete, Mini, EDTA-free is preferencially used in the isolation process of Poly-His tagged fusion proteins. cOmplete Mini, EDTA-free tablets inhibit efficiently serine and cysteine proteases in a broad range but not metalloproteases. Occasionally, aspartic proteases ...
... metal affinity chromatography) cOmplete, Mini, EDTA-free is preferencially used in the isolation process of Poly-His tagged fusion proteins. cOmplete Mini, EDTA-free tablets inhibit efficiently serine and cysteine proteases in a broad range but not metalloproteases. Occasionally, aspartic proteases ...
Secondary Metabolism Part 1: Introduction, Fatty Acids and
... Aldol and Claisen reactions occur by first generating an enolate • C-C bond formation reactions (frequently between two C2 acetate groups) • Base catalyzed (Enzyme mediated) • Formation of enolate followed by nucleophilic attack by enolate into carbonyl • Aldol vs. Claisen Products depend on LG ...
... Aldol and Claisen reactions occur by first generating an enolate • C-C bond formation reactions (frequently between two C2 acetate groups) • Base catalyzed (Enzyme mediated) • Formation of enolate followed by nucleophilic attack by enolate into carbonyl • Aldol vs. Claisen Products depend on LG ...
Finals Practice Exam answers
... I). Acid-Base Catalysis- Which enzyme of glycolysis uses a strict acid-base catalytic mechanism? What candidate amino acids would you expect this enzyme to use for this acid-base catalysis? II). Covalent Catalysis- Name a common covalent enzyme/substrate adduct (intermediate) that appears in glycoly ...
... I). Acid-Base Catalysis- Which enzyme of glycolysis uses a strict acid-base catalytic mechanism? What candidate amino acids would you expect this enzyme to use for this acid-base catalysis? II). Covalent Catalysis- Name a common covalent enzyme/substrate adduct (intermediate) that appears in glycoly ...
Enzymes - WordPress.com
... The active site of an enzyme binds the substrate molecule(s) of a biochemical reaction, and is critical to its specificity and catalytic activity. Many enzymes are specific for just one reaction. For example, catalase only catalyzes the breakdown of hydrogen peroxide, a toxic by-product of metabolis ...
... The active site of an enzyme binds the substrate molecule(s) of a biochemical reaction, and is critical to its specificity and catalytic activity. Many enzymes are specific for just one reaction. For example, catalase only catalyzes the breakdown of hydrogen peroxide, a toxic by-product of metabolis ...
Lecture 10 - Protein Turnover and Amino Acid
... The aldehyde forms a Schiff–base with an ε– amino group on the enzyme. This Schiff-bases can be exchanged for one with the α–amino group of an amino acid ...
... The aldehyde forms a Schiff–base with an ε– amino group on the enzyme. This Schiff-bases can be exchanged for one with the α–amino group of an amino acid ...
Biochemistry II Test 2Q
... The long chain fatty acids (__c), except for ___ are produced by FA elongation with _____. Where does FA elongation occur, what is its enzyme, substrate, and dependence? The short chain FAs have how many carbons? Since short chain production occurs in the mitochondria, the substrate is naturally ___ ...
... The long chain fatty acids (__c), except for ___ are produced by FA elongation with _____. Where does FA elongation occur, what is its enzyme, substrate, and dependence? The short chain FAs have how many carbons? Since short chain production occurs in the mitochondria, the substrate is naturally ___ ...
Chapter 6
... Active site (and R groups of its amino acids) can lower EA and speed up a reaction by • acting as a template for substrate orientation, • stressing the substrates and stabilizing the transition state, • providing a favorable microenvironment, • participating directly in the catalytic reaction. ...
... Active site (and R groups of its amino acids) can lower EA and speed up a reaction by • acting as a template for substrate orientation, • stressing the substrates and stabilizing the transition state, • providing a favorable microenvironment, • participating directly in the catalytic reaction. ...
Properties of Enzymes Lab
... Factors that Effect Enzyme Function Introduction: Enzymes are proteins that speed up chemical reactions by lowering the activation energy needed to start the reaction. They do this by binding to the reactants (substrates) and changing shape which places the substrates in a position that facilitates ...
... Factors that Effect Enzyme Function Introduction: Enzymes are proteins that speed up chemical reactions by lowering the activation energy needed to start the reaction. They do this by binding to the reactants (substrates) and changing shape which places the substrates in a position that facilitates ...
Design of Tight-Binding Human Immunodeficiency
... disease to mankind. Until this day, human immune deficiency virus, HIV, has caused the death of many humans and infected patients have little chance to become healthy. In the beginning, people become exposed to HIV mainly by unsafe sex with HIV positive person of the same sex. But the situation has ...
... disease to mankind. Until this day, human immune deficiency virus, HIV, has caused the death of many humans and infected patients have little chance to become healthy. In the beginning, people become exposed to HIV mainly by unsafe sex with HIV positive person of the same sex. But the situation has ...
Chapter 26:Biomolecules: Amino Acids, Peptides, and Proteins
... nitrogens are nonbasic because their unshared electron pair is delocalized by interaction with the carbonyl group. This overlap of the nitrogen p orbital with the π orbitals of the carbonyl group imparts a certain amount of double-bond character to the C–N bond and restricts rotation around it. The ...
... nitrogens are nonbasic because their unshared electron pair is delocalized by interaction with the carbonyl group. This overlap of the nitrogen p orbital with the π orbitals of the carbonyl group imparts a certain amount of double-bond character to the C–N bond and restricts rotation around it. The ...
Enzymes Review Game with Answers 2014 2015
... B) An enzyme's function is unaffected by changes in pH. C) Enzymes catalyze specific reactions. D) Enzymes slow down the rate of a chemical reaction. ...
... B) An enzyme's function is unaffected by changes in pH. C) Enzymes catalyze specific reactions. D) Enzymes slow down the rate of a chemical reaction. ...
Polymer Molecules
... All proteins contain the elements C,O,H, N. They are condensation polymers, made by amino acids linking together. An amine group of one molecule links to the carboxyl group of another molecule to form an amide or peptide bond. The body cannot make every type of amino acids that it needs. So our diet ...
... All proteins contain the elements C,O,H, N. They are condensation polymers, made by amino acids linking together. An amine group of one molecule links to the carboxyl group of another molecule to form an amide or peptide bond. The body cannot make every type of amino acids that it needs. So our diet ...
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.