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Chapter 15 Review Questions
Chapter 15 Review Questions

... a protein is its amino acid chain, bonded together with peptide bonds (amide linkages). The secondary structure of a protein begins to shape the amino acid chain using hydrogen bonding, forming alpha-helix and beta-pleated sheet structures. The tertiary structure of a protein gives it 3 dimensions. ...
Features of the DNA Double Helix - E
Features of the DNA Double Helix - E

... Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. The proteins in eggs denature and coagulate during cooking. Other foods ...
Enzyme Mechanisms: Serine Proteases Questions
Enzyme Mechanisms: Serine Proteases Questions

... C) distinct backbone conformations of the individual proteins. D) A and B.  E) A, B and C.  2. The role of serine at the active site of serine proteases is to act as a(n) ________ catalyst, while the  histidine residue serves as a(n) ________ catalyst.  A) strong; weak  B) weak; strong  C) acid‐base ...
Making and Using an Oligo Probe Labeled with Alkaline Phosphatase
Making and Using an Oligo Probe Labeled with Alkaline Phosphatase

...  During rinse, in the absence of additional probe, when an oligonucleotide separates from target, it won’t be replaced by another probe ...
Macromolecules - Van Buren Public Schools
Macromolecules - Van Buren Public Schools

... • Regular, repeating 3D segments of coils or folds • Form because of hydrogen bonding in the C/N backbone of the polypeptide chain (thus all proteins have similar secondary structure) – All proteins have the same C and N groups – Result of electronegativity! H’s attracted to O’s ...
Altering substrate specificity of catechol 2,3
Altering substrate specificity of catechol 2,3

... conserved region in the active site containing two histidine residues, one glutamate and two molecules of water as Fe2+ ligands (Huang et al., 2010; Wojcieszyńska et al., 2011). The catalytic mechanism starts with bidentate binding of the substrate as catecholate monoanion to the active-site metal w ...
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry

... of a bond between groups A and B: A-B + H2O  A + B In the presence of a covalent catalyst (an enzyme with the nucleophilic group X:) the reaction becomes 1) A-B + X:  A-X + B 2) A-X + H2O  A + X: This alters the pathway of the reaction, and it results in catalysis if the new pathway has a lower a ...
Macromolecules of Life – Lecture 1
Macromolecules of Life – Lecture 1

... c. Enzymes – each enzyme (made of protein) is regulated, with a special “job” i. Jobs include ii. Operate by “Lock and Key” approach iii. Hydrolysis – (Breaking down polysaccharides to create simple sugars) iv. Dehydration – removal of water to create complex compounds ...
CHAPTER OBJECTIVES Topic 1: Introduction 1. Know the
CHAPTER OBJECTIVES Topic 1: Introduction 1. Know the

Revised Higher Human Biology Unit 1 Revision Summary STEM
Revised Higher Human Biology Unit 1 Revision Summary STEM

... Other respiratory substrates, other than glucose, can be used to produce ATP. Both starch and glycogen (A storage carbohydrate in the liver) are made up of chains of glucose molecules. These carbohydrates can be broken down during respiration into glucose very quickly, to generate ATP. Maltose and s ...
File
File

AIM: What are Macromolecules?
AIM: What are Macromolecules?

... • All carbohydrates consist of C, H, and O combined in a very specific ratio : 1:2:1 (Means that for every atom of Carbon there are twice as many Hydrogen atoms and the same number of Oxygen atoms) ...
Chemistry of Life
Chemistry of Life

... Enzymes • Globular proteins acting as catalysts to speed a reaction – Lowers energy of activation (EA) ...
Biology Topic 2
Biology Topic 2

... its sugar polymers, glycogen in animals and starch in plants. These sugars are released when the demand for sugar increases. Animals use lipids, mainly fats, for long-term energy storage. ...
Coenzyme Q = Ubiquinone
Coenzyme Q = Ubiquinone

... sono necessari per visualizzare quest'immagine. ...
1. The formation of a peptide bond between two amino acids is an
1. The formation of a peptide bond between two amino acids is an

... 42. Which of the following statements about allosteric control of enzymatic activity is false? A) B) C) D) E) ...
BIO 212 SI Kukday--Energetics (2) Review 2/7
BIO 212 SI Kukday--Energetics (2) Review 2/7

... f. Blocking an enzyme as a result of feedback g. The process that turns acetyl CoA into NADH and FADH2 h. This process happens outside the mitochondria and turns glucose into pyruvate i. Inhibition that requires making a new enzyme to resume the process j. Process where most of the ATP is actually p ...
Irreversible Inhibition
Irreversible Inhibition

Metabolic Processes
Metabolic Processes

... The pleated sheet structure is often found in many structural proteins, such as "Fibroin", the protein in spider webs. ...
The Chemistry of Life
The Chemistry of Life

... Enzyme- Biological Catalyst Catalyst  a chemical agent that changes the rate of a reaction without being consumed by the reaction  Enzyme is a catalytic protein.  Enzymes provide a way for reactions to occur by lowering the activation energy  Activation Energy energy required to get a reaction ...
ch_12 - WordPress.com
ch_12 - WordPress.com

Biochemistry 2007
Biochemistry 2007

... The distance between the distal histidine residue HisE7 and the heme group iron ion. The hydrophilic nature of the hemoglobin molecule surface The tetrameric structure of hemoglobin ...
AP Bio A final exam study guide
AP Bio A final exam study guide

... Explain the difference between polar and nonpolar molecules relating this property to interactions with water molecules (hydrophilic vs. hydrophobic). Give examples. ...
Mitochondrial Lab - University of Colorado Denver
Mitochondrial Lab - University of Colorado Denver

... ATP or reduced coenzyme Q are allosteric activators of Succ Dehyd Allosteric activators typically bind somewhere between the subunits of Succ Dehyd (not the active site) to stimulate the enzyme activity Allosteric inhibitors act similarly to inhibit ...
Proteinases as catalysts in peptide synthesis
Proteinases as catalysts in peptide synthesis

... enzymes as a rule possess extended substrate binding sites that are capable of accommodating 6-8 amino acid residues. Therefore, their application to catalyze peptide bond formation between e.g, two amino acids, being interesting per se, often gives the results hardly relevant for genuine evaluation ...
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Enzyme



Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.
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