
active site - Blue Valley Schools
... Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. ...
... Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. ...
File - Mr. Shanks` Class
... How many times do we have to cut the 18 carbon fatty acid? C-C C-C C-C C-C C-C C-C C-C C-C C-C ...
... How many times do we have to cut the 18 carbon fatty acid? C-C C-C C-C C-C C-C C-C C-C C-C C-C ...
Chem*3560 Lecture 15: Gluconeogenesis
... Location of pyruvate carboxylase and PEP carboxykinase Pyruvate carboxylase is located in mitochondria, whereas PEP carboxykinase is located in both cytoplasm and in mitochondria. Which is used depends on the starting substrate used. When lactate is the starting substrate, lactate dehydrogenase pro ...
... Location of pyruvate carboxylase and PEP carboxykinase Pyruvate carboxylase is located in mitochondria, whereas PEP carboxykinase is located in both cytoplasm and in mitochondria. Which is used depends on the starting substrate used. When lactate is the starting substrate, lactate dehydrogenase pro ...
B7 Enzymes
... structures where all the charged (hydrophilic and hydrophobic) amino acids residues are paired. Many enzymes are absolutely specific for a particular substrate (not even an enantiomer), where others will react with a whole class of molecules but at widely different rates. ...
... structures where all the charged (hydrophilic and hydrophobic) amino acids residues are paired. Many enzymes are absolutely specific for a particular substrate (not even an enantiomer), where others will react with a whole class of molecules but at widely different rates. ...
Glycolysis Citric Acid Cycle Krebs Cycle Oxidative Phosphorylation
... The first half of the cycle occurs in many different tissues (like muscle) when lactate is formed from glucose during oxygen debt. Glucose → 2 Lactates Provides: 2 ATP from glycolysis The second half of the cycle converts lactate back into glucose. This takes place in the liver when plenty of oxygen ...
... The first half of the cycle occurs in many different tissues (like muscle) when lactate is formed from glucose during oxygen debt. Glucose → 2 Lactates Provides: 2 ATP from glycolysis The second half of the cycle converts lactate back into glucose. This takes place in the liver when plenty of oxygen ...
Enzyme Activity
... If another enzyme from a north sea crustacean was studied and its enzyme activity was plotted on the graph, where would it appear? If a hot springs bacterial enzyme was studied and its activity data was plotted, where would it lie? ...
... If another enzyme from a north sea crustacean was studied and its enzyme activity was plotted on the graph, where would it appear? If a hot springs bacterial enzyme was studied and its activity data was plotted, where would it lie? ...
N -glutamate Iminohydrolase from Pseudomonas aeruginosa L
... are found in every organism sequenced to date (4, 5) and are characterized by a mono- or binuclear metal center embedded within the C-terminal end of a (β/R)8 barrel structural fold (3). HutF most closely resembles the sequences possessed by enzymes that catalyze the deamination of the heterocyclic ...
... are found in every organism sequenced to date (4, 5) and are characterized by a mono- or binuclear metal center embedded within the C-terminal end of a (β/R)8 barrel structural fold (3). HutF most closely resembles the sequences possessed by enzymes that catalyze the deamination of the heterocyclic ...
Chapter 16 Citric Acid Cycle
... product for synthesis of other things, so has a central role in metabolism, and has complex control (you thought glycolysis was tough) 16.1 Production of acetate Several different ways compounds can enter the citric acid cycle. Many AA, pyruvate from glycolysis, and fatty acids enter as an acetate g ...
... product for synthesis of other things, so has a central role in metabolism, and has complex control (you thought glycolysis was tough) 16.1 Production of acetate Several different ways compounds can enter the citric acid cycle. Many AA, pyruvate from glycolysis, and fatty acids enter as an acetate g ...
Document
... concentration is increased up to a point where the enzyme is "saturated" with substrate. At this point the rate of the reaction (v) reaches a maximal value and is unaffected by further increases in substrate because all of the enzyme active site is bound to substrate ...
... concentration is increased up to a point where the enzyme is "saturated" with substrate. At this point the rate of the reaction (v) reaches a maximal value and is unaffected by further increases in substrate because all of the enzyme active site is bound to substrate ...
... 4. A small 20 residue peptide will be largely found buried in a phospholipid bilayer membrane if: a) its sidechains are all protons (e.g. glycine). (+1/2 pt) b) its sidechains are all CH2-OH groups (e.g. Serine). c) its sidechains are all CH3 groups (e.g. Alanine). (+1 pt) [Alanine is not sufficient ...
Lecture 2: Glycolysis Part 1 - Berkeley MCB
... Energetics. Large free energy change typical of kinase due to the phosphoryl transfer potential of ATP, generating a low energy phosphate bond at about 12 kJ/mol. Downhill reaction. PFK Regulation & The Pasteur Effect. The fact that PFK is important in regulation came from the old experiments of Lou ...
... Energetics. Large free energy change typical of kinase due to the phosphoryl transfer potential of ATP, generating a low energy phosphate bond at about 12 kJ/mol. Downhill reaction. PFK Regulation & The Pasteur Effect. The fact that PFK is important in regulation came from the old experiments of Lou ...
Cell Respiration
... At 3 points along the chain enough energy is given up for ATP to be made by the enzyme ATP synthetase. This process is called OXIDATIVE PHOSPHORYLATION. FADH2 also feeds e- into the ETC, but at a later stage than NADH, resulting in 2 ATP molecules instead of 3. ...
... At 3 points along the chain enough energy is given up for ATP to be made by the enzyme ATP synthetase. This process is called OXIDATIVE PHOSPHORYLATION. FADH2 also feeds e- into the ETC, but at a later stage than NADH, resulting in 2 ATP molecules instead of 3. ...
Spring 2016 Practice Final Exam w/ solution
... e (2 pts). How many ATP molecules are needed to fix a molecule of CO2 in (i) C3 plant (normal plant) and (ii) in a C4 plant? Ans: (i) 3 ATPs (ii) 5 ATPs f (2 pts). The net reaction for oxidative phosphorylation can be written as: 2NADH + 2H+ + O2 → 2H2O + 2NAD+ Write an analogous equation for the li ...
... e (2 pts). How many ATP molecules are needed to fix a molecule of CO2 in (i) C3 plant (normal plant) and (ii) in a C4 plant? Ans: (i) 3 ATPs (ii) 5 ATPs f (2 pts). The net reaction for oxidative phosphorylation can be written as: 2NADH + 2H+ + O2 → 2H2O + 2NAD+ Write an analogous equation for the li ...
Page 1 - csfcbiology
... Aspirin is a very useful drug. One of its uses is to reduce fever and inflammation. Aspirin does this by preventing cells from producing substances called prostaglandins. Prostaglandins are produced by an enzyme-controlled pathway. Aspirin works by inhibiting one of the enzymes in this pathway. Aspi ...
... Aspirin is a very useful drug. One of its uses is to reduce fever and inflammation. Aspirin does this by preventing cells from producing substances called prostaglandins. Prostaglandins are produced by an enzyme-controlled pathway. Aspirin works by inhibiting one of the enzymes in this pathway. Aspi ...
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI
... (b) Discuss the substrate specificity of enzymes and the different ways in which substrate can be affected when at the active site. 22(a) Describe zymogens with suitable examples. OR (b) Write notes on: (i) Catalytic mechanism of tryptophan synthase (ii) Substrate binding by chymotrypsin and trypsin ...
... (b) Discuss the substrate specificity of enzymes and the different ways in which substrate can be affected when at the active site. 22(a) Describe zymogens with suitable examples. OR (b) Write notes on: (i) Catalytic mechanism of tryptophan synthase (ii) Substrate binding by chymotrypsin and trypsin ...
Oxidative Decarboxylation and Krebs Cycle
... 1.When NADH is oxidized in the ETC 3 ATP molecules, (this is oxidative phosphorylation). 2.which when FADH oxidized in the ETC 2 ATP (this is oxidative phosphorylation). 3. In substrate-level phosphorylation NO need for o2 and/or mitochondria.. And we have only one reaction in krebs cycle can do ...
... 1.When NADH is oxidized in the ETC 3 ATP molecules, (this is oxidative phosphorylation). 2.which when FADH oxidized in the ETC 2 ATP (this is oxidative phosphorylation). 3. In substrate-level phosphorylation NO need for o2 and/or mitochondria.. And we have only one reaction in krebs cycle can do ...
Substrate Level Phosphorylation Substrate level phosphorylation
... • The substance being reduced actually gets “bigger” because the increased number of electrons allows for more bonds • Glucose oxidation transfers electrons (of hydrogen) to a lower energy state as it bonds with oxygen – Energy released is used in ATP regeneration ...
... • The substance being reduced actually gets “bigger” because the increased number of electrons allows for more bonds • Glucose oxidation transfers electrons (of hydrogen) to a lower energy state as it bonds with oxygen – Energy released is used in ATP regeneration ...
12.3 The Citric Acid Cycle Oxidizes AcetylCoA
... atoms in the cycle • Carbon atoms from acetyl CoA (red) are not lost in the first turn of the cycle ...
... atoms in the cycle • Carbon atoms from acetyl CoA (red) are not lost in the first turn of the cycle ...
Practice Exam III
... a). Enzymes theoretically stabilize the transition state of the reaction they catalyze. b). Enzymes alter the equilibrium distribution of the substrate(s) and product(s) of the reaction they catalyze. c). Enzymes reduce the activation energy of the reaction they catalyze. d). Enzymes employ a wide v ...
... a). Enzymes theoretically stabilize the transition state of the reaction they catalyze. b). Enzymes alter the equilibrium distribution of the substrate(s) and product(s) of the reaction they catalyze. c). Enzymes reduce the activation energy of the reaction they catalyze. d). Enzymes employ a wide v ...
BS 11 First Mid-Term Answer Key Spring 1998
... (2 pt) L) Mutation of S195, H57 and D102 of chymotrypsin to alanine residues yields an enzyme that enhances proteolysis rates by ~5x104 over the uncatalyzed reaction. The native enzyme has a rate enhancement factor of ~1010. The explanation for the rate enhancement by the mutated enzyme is: a) The m ...
... (2 pt) L) Mutation of S195, H57 and D102 of chymotrypsin to alanine residues yields an enzyme that enhances proteolysis rates by ~5x104 over the uncatalyzed reaction. The native enzyme has a rate enhancement factor of ~1010. The explanation for the rate enhancement by the mutated enzyme is: a) The m ...
Chapter 20 Enzymes and Vitamins
... Enzyme Catalyzed Reaction: Basic Mechanism The proper fit of a substrate (S) in an active site forms an enzyme-substrate (ES) complex. E+S ES Within the ES complex, the reaction occurs to convert substrate to product (P). ...
... Enzyme Catalyzed Reaction: Basic Mechanism The proper fit of a substrate (S) in an active site forms an enzyme-substrate (ES) complex. E+S ES Within the ES complex, the reaction occurs to convert substrate to product (P). ...
Luciferase

Luciferase is a generic term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. The name is derived from Lucifer, the root of which means 'light-bearer' (lucem ferre). One example is the firefly luciferase (EC 1.13.12.7) from the firefly Photinus pyralis. ""Firefly luciferase"" as a laboratory reagent often refers to P. pyralis luciferase although recombinant luciferases from several other species of fireflies are also commercially available.