Bio102 Problems
... each of these oxidations, a reduced coenzyme is produced which will ultimately be used to synthesize more ATP by oxidative phosphorylation. 16. The AMPK enzyme becomes active when A. PFK activity is inhibited. B. AMP concentrations are high. C. oxygen is abundant. D. Photosystem II is inhibited. E. ...
... each of these oxidations, a reduced coenzyme is produced which will ultimately be used to synthesize more ATP by oxidative phosphorylation. 16. The AMPK enzyme becomes active when A. PFK activity is inhibited. B. AMP concentrations are high. C. oxygen is abundant. D. Photosystem II is inhibited. E. ...
Enzyme Activity
... • Km : Non-competitive inhibitors do not interfere with the binding of substrate to enzyme. • Thus, the enzyme shows the same Km in the presence or absence of the non-competitive inhibitor. • Vmax: Increasing the concentration of substrate does not overcome non-competitive inhibition. • Non-competi ...
... • Km : Non-competitive inhibitors do not interfere with the binding of substrate to enzyme. • Thus, the enzyme shows the same Km in the presence or absence of the non-competitive inhibitor. • Vmax: Increasing the concentration of substrate does not overcome non-competitive inhibition. • Non-competi ...
5-MGD Session 3, Lec 5, 2014
... Some enzymes also require the presence of additional chemical components to catalyse reactions. *Cofactors are inorganic ions such as Fe2+, Mn2+etc. *Coenzymes are organic compounds that act as temporary carriers of groups in the reaction e.g. nicotinamide ...
... Some enzymes also require the presence of additional chemical components to catalyse reactions. *Cofactors are inorganic ions such as Fe2+, Mn2+etc. *Coenzymes are organic compounds that act as temporary carriers of groups in the reaction e.g. nicotinamide ...
5_Bio_1_ReKaps
... Uncompetitive: inhibitor binds reversibly to a site which only becomes available after the substrate has bound to the active site of the enzyme Irreversible: inhibitor binds permanently to active site or otherwise destroys the enzyme Negative Feedback: inhibition of a reaction pathway due to acc ...
... Uncompetitive: inhibitor binds reversibly to a site which only becomes available after the substrate has bound to the active site of the enzyme Irreversible: inhibitor binds permanently to active site or otherwise destroys the enzyme Negative Feedback: inhibition of a reaction pathway due to acc ...
Table S2
... Sic1: Inhibitor of Clb-Cdc28. Phosphorylation of Sic1 by Cln-Cdc28 as well as Pcl1-Pho85 cyclin dependent kinase is necessary; phosphorylation leads to ubiquitin-dependent degradation of Sic1, which allows the cell to pass Start. In vitro and in vivo phosphorylation sites have been mapped using mass ...
... Sic1: Inhibitor of Clb-Cdc28. Phosphorylation of Sic1 by Cln-Cdc28 as well as Pcl1-Pho85 cyclin dependent kinase is necessary; phosphorylation leads to ubiquitin-dependent degradation of Sic1, which allows the cell to pass Start. In vitro and in vivo phosphorylation sites have been mapped using mass ...
Enzymes
... Factors that effect enzyme activity Vmax this is the fastest number of substrates an enzyme can process Competitive inhibitors: look like the enzymes substrate so they block up the active site More substrate can reduce their effects substrate ...
... Factors that effect enzyme activity Vmax this is the fastest number of substrates an enzyme can process Competitive inhibitors: look like the enzymes substrate so they block up the active site More substrate can reduce their effects substrate ...
Chap. 6B Enzymes Introduction to Enzymes How Enzymes Work
... Substrate-activity curves for representative allosteric enzymes that show complex responses to their modulators are shown in Fig. 6-34. In Panel (a), the sigmoid curve is for a homotropic enzyme, for which the substrate also serves as a positive modulator. This curve (black) resembles the oxygen-sat ...
... Substrate-activity curves for representative allosteric enzymes that show complex responses to their modulators are shown in Fig. 6-34. In Panel (a), the sigmoid curve is for a homotropic enzyme, for which the substrate also serves as a positive modulator. This curve (black) resembles the oxygen-sat ...
poster - Computer Science and Engineering
... from different species covering 1372 Tyr, 3175 Ser and 767 Thr experimentally verified phosphorylation sites manually curated from the literature. We constructed separate data sets for kinase families that are well represented in terms of the data available in the database (i.e., they are known to r ...
... from different species covering 1372 Tyr, 3175 Ser and 767 Thr experimentally verified phosphorylation sites manually curated from the literature. We constructed separate data sets for kinase families that are well represented in terms of the data available in the database (i.e., they are known to r ...
Answer: ( c ) Relative specificity One of the main characteristics
... One of the main characteristics of enzymes is their high specificity. Enzymes are specific for: a) the substrate b) the reaction It means that they catalyze the transformation of just one substrate or a family of substrates that are structurally related, catalyzing only one of the possible reactions ...
... One of the main characteristics of enzymes is their high specificity. Enzymes are specific for: a) the substrate b) the reaction It means that they catalyze the transformation of just one substrate or a family of substrates that are structurally related, catalyzing only one of the possible reactions ...
31P n.m.r. analysis of the renal response to respiratory acidosis
... 2.2s, unidentified peak at 11.1 p.p.m. (including AMP) 1 . 9 ~ 1 gave absolute values for adenine nucleotides and phosphate which differ significantly from those obtained by enzymic assay in the same kidney. The differences cannot be explained as artifacts from breakdown of the normal renal constitu ...
... 2.2s, unidentified peak at 11.1 p.p.m. (including AMP) 1 . 9 ~ 1 gave absolute values for adenine nucleotides and phosphate which differ significantly from those obtained by enzymic assay in the same kidney. The differences cannot be explained as artifacts from breakdown of the normal renal constitu ...
Chapter 6
... Control of enzyme availability • Amount of given enzyme in a cell depends on its rate of synthesis and its rate of degradation Control of enzyme activity • Catalytic activity controlled through structural alteration ...
... Control of enzyme availability • Amount of given enzyme in a cell depends on its rate of synthesis and its rate of degradation Control of enzyme activity • Catalytic activity controlled through structural alteration ...
Assignment 5 Bioenergy/ Photosynthesis
... hydrogen bonds or ionic interactions, the enzyme can change its conformation to move the reactants into a position to react (e.g. split the reactant apart, put two reactants together, or change the reactivity or shape of the reactant). The amount of energy required for the reaction to proceed withou ...
... hydrogen bonds or ionic interactions, the enzyme can change its conformation to move the reactants into a position to react (e.g. split the reactant apart, put two reactants together, or change the reactivity or shape of the reactant). The amount of energy required for the reaction to proceed withou ...
Biochemistry I, Spring Term 2001 - Second Exam answer key
... Since the Km observed in the presence of the inhibitor is αKm, you need to find the Km in the presence of the inhibitor. Again, there are two ways of doing this, from the xintercept or the slope. Using the slopes is easiest, since the ratio of the two slopes (with and without inhibitor) is α. The ra ...
... Since the Km observed in the presence of the inhibitor is αKm, you need to find the Km in the presence of the inhibitor. Again, there are two ways of doing this, from the xintercept or the slope. Using the slopes is easiest, since the ratio of the two slopes (with and without inhibitor) is α. The ra ...
Bio-chemistry(Enzymes)
... Order of reaction: When the velocity of the reaction is almost proportional to the substrate concentration (i.e. [S] is less than Km,) the rate of the reaction is said to be first order with respect to substrate. When the [S] is much greater than Km, the rate of reaction is independent of substrate ...
... Order of reaction: When the velocity of the reaction is almost proportional to the substrate concentration (i.e. [S] is less than Km,) the rate of the reaction is said to be first order with respect to substrate. When the [S] is much greater than Km, the rate of reaction is independent of substrate ...
Revealing kinase inhibitor mechanisms: ITC leads the way
... Elucidation of mechanism As with all therapeutically important enzymes, kinases are not just a single molecular target for compound intervention. During the catalytic cycle the kinase binds protein substrate, ATP, intermediates, and products, (Fig 2). These different enzyme forms may also exist in m ...
... Elucidation of mechanism As with all therapeutically important enzymes, kinases are not just a single molecular target for compound intervention. During the catalytic cycle the kinase binds protein substrate, ATP, intermediates, and products, (Fig 2). These different enzyme forms may also exist in m ...
SUCCINYL-CoA SYNTHETASE from a prokaryote (Lot 140901b)
... - One major bands on isoelectric focusing (pI ~ 5.9) ...
... - One major bands on isoelectric focusing (pI ~ 5.9) ...
Unit 04 Enzymes and respiration Review
... 10. Summarize in order the parts of aerobic respiration ( Krebs cycle, glycolysis, ETC). Tell what is produced in each part. 11. When do we notice plants using respiration pathways? Is this the only time they respire? 12. How could we tell that plants were using respiration? 13. Name an organism tha ...
... 10. Summarize in order the parts of aerobic respiration ( Krebs cycle, glycolysis, ETC). Tell what is produced in each part. 11. When do we notice plants using respiration pathways? Is this the only time they respire? 12. How could we tell that plants were using respiration? 13. Name an organism tha ...
Enzymes - Website of Neelay Gandhi
... amt of enzyme needed for 1 micromol of substrate into products in one minute (std conditions) mole of substrate consumed or product formed per second Enzyme activity / protein concentration (for enzyme purity) measure of maximal catalytic activity Number of substrate molecules converted into produce ...
... amt of enzyme needed for 1 micromol of substrate into products in one minute (std conditions) mole of substrate consumed or product formed per second Enzyme activity / protein concentration (for enzyme purity) measure of maximal catalytic activity Number of substrate molecules converted into produce ...
3-1 Cyclin-Dependent Kinases
... The cyclin-dependent kinases (Cdks) are a family of serine/threonine protein kinases whose members are small proteins (~34–40 kDa) composed of little more than the catalytic core shared by all protein kinases. By definition, all Cdks share the feature that their enzymatic activation requires the bin ...
... The cyclin-dependent kinases (Cdks) are a family of serine/threonine protein kinases whose members are small proteins (~34–40 kDa) composed of little more than the catalytic core shared by all protein kinases. By definition, all Cdks share the feature that their enzymatic activation requires the bin ...
ENZYMES PPT
... The enzyme’s active site changes shape so that a second substrate molecule can bind The second substrate binds Chemical process (rx) occurs ...
... The enzyme’s active site changes shape so that a second substrate molecule can bind The second substrate binds Chemical process (rx) occurs ...
ENZYMES: THE MAJESTIC MOLECULES OF LIFE Part
... suggested that weak-bonding interactions between an enzyme and its substrate(s) might be used to distort the substrate and catalyze a reaction. This insight lies at the heart of our current understanding of enzymology. In the latter part of the 20th Century, research on the enzymes of cellular meta ...
... suggested that weak-bonding interactions between an enzyme and its substrate(s) might be used to distort the substrate and catalyze a reaction. This insight lies at the heart of our current understanding of enzymology. In the latter part of the 20th Century, research on the enzymes of cellular meta ...
01_Introduction. Structure, properties and biological functions
... Allosteric enzymes contain more than one polypeptide chain (have quaternary structure). Allosteric modulators bind noncovalently to allosteric site and regulate enzyme activity via conformational changes ...
... Allosteric enzymes contain more than one polypeptide chain (have quaternary structure). Allosteric modulators bind noncovalently to allosteric site and regulate enzyme activity via conformational changes ...
Ultrasensitivity
In molecular biology, ultrasensitivity describes an output response that is more sensitive to stimulus change than the hyperbolic Michaelis-Menten response. Ultrasensitivity is one of the biochemical switches in the cell cycle and has been implicated in a number of important cellular events, including exiting G2 cell cycle arrests in Xenopus laevis oocytes, a stage to which the cell or organism would not want to return.Ultrasensitivity is a cellular system which triggers entry into a different cellular state. Ultrasensitivity gives a small response to first input signal, but an increase in the input signal produces higher and higher levels of output. This acts to filter out noise, as small stimuli and threshold concentrations of the stimulus (input signal) is necessary for the trigger which allows the system to get activated quickly. Ultrasensitive responses are represented by sigmoidal graphs, which resemble cooperativity. Quantification of ultrasensitivity is often approximated by the Hill equation (biochemistry):Response= Stimulus^n/(EC50^n+Stimulus^n)Where Hill's coefficient (n) may represent quantitative measure of ultrasensitive response.