answer key
... Note that (v) is incorrect because the Km is not Vmax/2; the Km is the substrate concentration at which the reaction rate is Vmax/2. I. Glycolysis differs from the Krebs cycle in all of the following ways except [based on review sheet questions #5255] i. the Krebs cycle produces GTP and glycolysis p ...
... Note that (v) is incorrect because the Km is not Vmax/2; the Km is the substrate concentration at which the reaction rate is Vmax/2. I. Glycolysis differs from the Krebs cycle in all of the following ways except [based on review sheet questions #5255] i. the Krebs cycle produces GTP and glycolysis p ...
Evolution of Enzymatic Activity in the Enolase Superfamily: Structural
... an accidental racemization of N-acylamino acids [Palmer, D. R., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999) Biochemistry 38, 4252-4258]. To understand the molecular basis of this promiscuity, three-dimensional structures of liganded complexes of this enzyme ha ...
... an accidental racemization of N-acylamino acids [Palmer, D. R., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999) Biochemistry 38, 4252-4258]. To understand the molecular basis of this promiscuity, three-dimensional structures of liganded complexes of this enzyme ha ...
1 The diagram below represents a biological process 5
... for a few minutes, and then cooled. Which statement most likely explains why the boiled corn kernels remain sweet? 1) Boiling destroys sugar molecules so they cannot be converted to starch. 2) Boiling kills a fungus on the corn that is needed to convert sugar to starch. 3) Boiling activates the enzy ...
... for a few minutes, and then cooled. Which statement most likely explains why the boiled corn kernels remain sweet? 1) Boiling destroys sugar molecules so they cannot be converted to starch. 2) Boiling kills a fungus on the corn that is needed to convert sugar to starch. 3) Boiling activates the enzy ...
Prof. Kamakaka`s Lecture 12 Notes
... Role of the citric acid cycle in anabolism. Intermediates of the citric acid cycle are drawn off as precursors in many biosynthetic pathways. Shown in red are four anaplerotic reactions that replenish depleted cycle intermediates ...
... Role of the citric acid cycle in anabolism. Intermediates of the citric acid cycle are drawn off as precursors in many biosynthetic pathways. Shown in red are four anaplerotic reactions that replenish depleted cycle intermediates ...
Chem 352 - Fall 2014 - Exam II
... moiety that is very hydrophobic, along with a moiety that is at the same time very hydrophilic. When placed in water these molecules will aggregate in away that satisfies both of these characteristics. Phospholipids form lipid bilayers, in which the surfaces of the bilayer expose the hydrophilic moi ...
... moiety that is very hydrophobic, along with a moiety that is at the same time very hydrophilic. When placed in water these molecules will aggregate in away that satisfies both of these characteristics. Phospholipids form lipid bilayers, in which the surfaces of the bilayer expose the hydrophilic moi ...
1. Given the following metabolic pathway (as it occurs in the cell): a
... what you know about metabolism in other organisms, where would you expect this carbon to end up in the compounds shown at the right? Circle each carbon that could be labeled. ...
... what you know about metabolism in other organisms, where would you expect this carbon to end up in the compounds shown at the right? Circle each carbon that could be labeled. ...
Structural Insights into Catalysis and Inhibition of O
... enzymes. Serine acetyl transferase (SAT,3 EC 2.3.1.30), also denoted CysE, catalyzes the formation of O-acetylserine (OAS) from acetyl-CoA and serine. This metabolite is then converted to cysteine through the elimination of acetate and addition of hydrogen sulfide by the enzyme O-acetylserine sulfhy ...
... enzymes. Serine acetyl transferase (SAT,3 EC 2.3.1.30), also denoted CysE, catalyzes the formation of O-acetylserine (OAS) from acetyl-CoA and serine. This metabolite is then converted to cysteine through the elimination of acetate and addition of hydrogen sulfide by the enzyme O-acetylserine sulfhy ...
Understanding an Enzyme Active Site
... Protein secondary structure (alpha helices and beta sheets) provides that stable scaffolding upon which the critical active site amino acids can be precisely positioned in 3D space. The 2-3 amino acids that come together in 3D space to create an enzyme active site are very far apart in the linear se ...
... Protein secondary structure (alpha helices and beta sheets) provides that stable scaffolding upon which the critical active site amino acids can be precisely positioned in 3D space. The 2-3 amino acids that come together in 3D space to create an enzyme active site are very far apart in the linear se ...
6_Enzymes - WordPress.com
... molecule is unstable in this active conformation and tends to revert to its free form in the absence of substrate. In the induced fit model, the substrate induces a conformational change in the enzyme which aligns the amino acid residues or other groups for substrate binding, catalysis or both. (Fig ...
... molecule is unstable in this active conformation and tends to revert to its free form in the absence of substrate. In the induced fit model, the substrate induces a conformational change in the enzyme which aligns the amino acid residues or other groups for substrate binding, catalysis or both. (Fig ...
Lecture 13
... for reduction >10-12 use the pro-R hydrogen while those reactions with a Keq <10-10 use the pro-S hydrogen. The reasons for this are still unclear ...
... for reduction >10-12 use the pro-R hydrogen while those reactions with a Keq <10-10 use the pro-S hydrogen. The reasons for this are still unclear ...
Colorimetric End-Point Determination
... that enable the necessary metabolic reactions to occur at body temperature. Enzymes are the functional proteins that catalyze biological reactions. Enzyme catalysts are not used up in the process and do not change the equilibrium point of the reaction; they merely accelerate the rate for reaching eq ...
... that enable the necessary metabolic reactions to occur at body temperature. Enzymes are the functional proteins that catalyze biological reactions. Enzyme catalysts are not used up in the process and do not change the equilibrium point of the reaction; they merely accelerate the rate for reaching eq ...
File - Mr. Shanks` Class
... b) They function best at specific temperatures but break down at high temperatures. c) Some enzymes need activators or cofactors. d) They function best at a particular pH. e) They undergo major chemical change after reacting with their specific substrate. 5. The activity of an enzyme can be altered ...
... b) They function best at specific temperatures but break down at high temperatures. c) Some enzymes need activators or cofactors. d) They function best at a particular pH. e) They undergo major chemical change after reacting with their specific substrate. 5. The activity of an enzyme can be altered ...
Enzymes–II
... If, however, the effect of increasing temperature (in terms of three ill-demarcated categories of low, medium and high) on enzyme activity is studied (Fig. 17−6), it may be observed that the initial velocity of the reaction (given by the shape of the curves at t = 0) steadily increases with temperau ...
... If, however, the effect of increasing temperature (in terms of three ill-demarcated categories of low, medium and high) on enzyme activity is studied (Fig. 17−6), it may be observed that the initial velocity of the reaction (given by the shape of the curves at t = 0) steadily increases with temperau ...
f212 biological molecules
... • Folding of the polypeptide to give a more complex 3-D shape, the shape is specific to the function of the polypeptide. • Examples – Hormone must fit into the hormone receptor in a target cell – Enzymes have a complementary active site to it’s substrate ...
... • Folding of the polypeptide to give a more complex 3-D shape, the shape is specific to the function of the polypeptide. • Examples – Hormone must fit into the hormone receptor in a target cell – Enzymes have a complementary active site to it’s substrate ...
Kofaktörler - mustafaaltinisik.org.uk
... • Metal ions of metalloenzymes – cations that are tightly bound to enzyme and participate directly in catalysis (Fe, Zn, Cu, Co). • Metal activated enzymes – require or are stimulated by addition of metal ions (i.e. Mg2+, is required by many ATP requiring enzymes) ...
... • Metal ions of metalloenzymes – cations that are tightly bound to enzyme and participate directly in catalysis (Fe, Zn, Cu, Co). • Metal activated enzymes – require or are stimulated by addition of metal ions (i.e. Mg2+, is required by many ATP requiring enzymes) ...
Sample pages 2 PDF
... Amino acids can form amide bonds by condensation between carboxyl group and amino group as shown in Fig. 2.1. The amide bonds are specifically called the peptide bonds. If two amino acids are condensed, the product is called as dipeptide. When another amino acid condenses to this dipeptide, a tripep ...
... Amino acids can form amide bonds by condensation between carboxyl group and amino group as shown in Fig. 2.1. The amide bonds are specifically called the peptide bonds. If two amino acids are condensed, the product is called as dipeptide. When another amino acid condenses to this dipeptide, a tripep ...
Protein synthesis
... Some enzymes contain sites that bind cofactors, which are needed for catalysis. Certain enzymes have binding sites for small molecules, which are often direct or indirect products or substrates of the reaction catalyzed. This binding can serve to increase or decrease the enzyme's activity (depending ...
... Some enzymes contain sites that bind cofactors, which are needed for catalysis. Certain enzymes have binding sites for small molecules, which are often direct or indirect products or substrates of the reaction catalyzed. This binding can serve to increase or decrease the enzyme's activity (depending ...
Enzymes - Ústav lékařské biochemie a laboratorní diagnostiky
... with iodine at all (achrodextrin). At the same time the amount of reducing sugars in the hydrolytic mixture increases. β-Amylase is an enzyme of plant origin, contained also in malt, and splits 1,4-αglycosidic bonds from the non-reducing end of polysaccharide chain. Thus amylose gives practically qu ...
... with iodine at all (achrodextrin). At the same time the amount of reducing sugars in the hydrolytic mixture increases. β-Amylase is an enzyme of plant origin, contained also in malt, and splits 1,4-αglycosidic bonds from the non-reducing end of polysaccharide chain. Thus amylose gives practically qu ...
Publication JournalArticle (Originalarbeit in einer wissenschaftlichen
... responsible for the degradation of the inhibitory neurotransmitter GABA. GABA-AT is a validated target for antiepilepsy drugs because its selective inhibition raises GABA concentrations in brain. The antiepilepsy drug, gamma-vinyl-GABA (vigabatrin) has been investigated in the past by various bioche ...
... responsible for the degradation of the inhibitory neurotransmitter GABA. GABA-AT is a validated target for antiepilepsy drugs because its selective inhibition raises GABA concentrations in brain. The antiepilepsy drug, gamma-vinyl-GABA (vigabatrin) has been investigated in the past by various bioche ...
Protein structure and function
... side chains on the surface of the triple-helical molecule. [Note: This allows bond formation between the exposed R-groups of neighboring collagen monomers, resulting in their aggregation into long fibers.] 3. Hydroxyproline and hydroxylysine: Collagen contains hydroxyproline (hyp) and hydroxylysine ...
... side chains on the surface of the triple-helical molecule. [Note: This allows bond formation between the exposed R-groups of neighboring collagen monomers, resulting in their aggregation into long fibers.] 3. Hydroxyproline and hydroxylysine: Collagen contains hydroxyproline (hyp) and hydroxylysine ...
solute - Life Science Academy
... 5.15 A specific enzyme catalyzes each cellular reaction ◦ Enzymes have unique three-dimensional shapes that determine which chemical reactions occur in a cell ...
... 5.15 A specific enzyme catalyzes each cellular reaction ◦ Enzymes have unique three-dimensional shapes that determine which chemical reactions occur in a cell ...
Enzyme inhibitor
An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. They are also used in pesticides. Not all molecules that bind to enzymes are inhibitors; enzyme activators bind to enzymes and increase their enzymatic activity, while enzyme substrates bind and are converted to products in the normal catalytic cycle of the enzyme.The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation). These inhibitors modify key amino acid residues needed for enzymatic activity. In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind to the enzyme, the enzyme-substrate complex, or both.Many drug molecules are enzyme inhibitors, so their discovery and improvement is an active area of research in biochemistry and pharmacology. A medicinal enzyme inhibitor is often judged by its specificity (its lack of binding to other proteins) and its potency (its dissociation constant, which indicates the concentration needed to inhibit the enzyme). A high specificity and potency ensure that a drug will have few side effects and thus low toxicity.Enzyme inhibitors also occur naturally and are involved in the regulation of metabolism. For example, enzymes in a metabolic pathway can be inhibited by downstream products. This type of negative feedback slows the production line when products begin to build up and is an important way to maintain homeostasis in a cell. Other cellular enzyme inhibitors are proteins that specifically bind to and inhibit an enzyme target. This can help control enzymes that may be damaging to a cell, like proteases or nucleases. A well-characterised example of this is the ribonuclease inhibitor, which binds to ribonucleases in one of the tightest known protein–protein interactions. Natural enzyme inhibitors can also be poisons and are used as defences against predators or as ways of killing prey.