BIOM 250 1st Edition Lecture 5Outline of Last Lecture I. Gram Negative Cell WallII. Movement Across MembranesIII. Bacterial Cytoplasm StructuresIV. Eukaryotic CellOutline of Current Lecture I. OrganellesII. Microbial MetabolismIII. Chemical ReactionsIV. EnzymesCurrent LectureI. Organellesa. Nucleus- encloses nucleic acidi. Nuclear envelope with nuclear poresii. Has nucleoli, which is the site of rRNA synthesisb. Endoplasmic reticulum-i. Flattened membrane sacs/tubules called cisternaeii. Rough ER has bound ribosomesiii. Smooth ER has no bound ribosomes1. Functions in synthesizing lipids and sterolsc. Golgi complex- looks like a stack of pancakesi. Vesicles transport proteins in and glycosylates them1. Glycosylation- when sugars are attached to the proteinsii. Secretory vesicles send glycoproteins to membrane for incorporation/secretiond. Mitochondria- site of ATP productioni. Amount varies by cell typeThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.ii. Have a double membrane- outer is smooth, inner is folded into cristae and is filled with a semi-fluid matrixiii. Has its own genomee. Chloroplast- photosynthetic organi. Chlorophyll and photosynthetic enzymes in flattened sacsf. Lysosomes- single membrane enclosure with digestive enzymesi. Breaks down nutrients and bacteria g. Peroxisomes- smaller than but similar to lysosomesi. Has enzymes that oxidize organics (fats and amino acids)ii. Oxidation produces H202 (hydrogen peroxide) and catalase decomposes itiii. Oxidation- has NOTHING to do with oxygen1. It is the breaking of bonds and removal of electronsII. Microbial Metabolisma. Metabolism- the sum of chemical reactions in an organismi. They either release or require energyii. Often linked to ATP breakdown or formationb. Catabolism- catabolic/degradative reactions are where bonds are broken and energy is produced (exergonic)c. Anabolism- anabolic/biosynthetic reactions are where bonds are formed and energy is consumed (endergonic)III. Chemical reactions-a. The collision theory states that chemical reactions can occur when atoms, ions, or molecules collideb. Activation energy- needed to disrupt electronic bond configurationsc. Reaction rate- frequency of collisions with enough energy to bring about a reactioni. Can be increased by increasing temperature or pressure or with enzymesIV. Enzymesa. Lowers activation energy of reactionb. Enzyme process:i. Contains an active site that interacts with a specific substance called the substrateii. Temporary enzyme-substrate complex formsiii. Substrate(s) is properly orientediv. Enzyme changes conformationv. Bonds broken and/or formedvi. Products are made and then released as the enzyme goes back to its initial conformation c. Components- usually all protein, some have accessory factorsi. Apoenzyme (protein) links with a cofactor (Fe, Zn, Mg, Ca) or coenzyme (organic molecule)ii. Without cofactors/coenzymes the enzyme is inactiveiii. Coenzymes often are derivatives of vitaminsd. Turnover number- the max number of substrate molecules formed per second byan enzymei. Example- lactate dehydrogenase produces 1000 reactions per seconde. Enzyme Classification:i. Oxidoreductase: oxidation-reduction reactionsii. Transferase- transfer functional groupsiii. Hydrolase- hydrolysis (add water)iv. Isomerase- rearrangement of atomsv. Ligase- joining of molecules using ATPf. Enzyme inhibitorsi. Competitive inhibitors- bind to active siteii. Non-competitive inhibitors- do not bind to active site but to an allosteric site which may change the enzyme shape and inactivate it1. Allosteric site is another site besides the active