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INDUSTRIAL BIOTECHNOLOGY BASICS History of Biotechnology What is Biotechnology? Biotechnology is a field of applied biology that involves the use of living organisms and bioprocesses in engineering, technolgy, medicine and other fields requiring bioproducts. Modern use similar term includes genetic engineering as well as cell- and tissue culture t h l i technologies. BIOLOGY BioBio chemist ry Bioengineering CHEMISTRY Chemistryg g engineering ENGINEERING Classification of Biotechnology Red Biotechnology Green Biotechnology is applied to medical processes. is biotechnology applied to agricultural processes. Some examples are the designing of organisms to produce antibiotics, and the engineering of genetic cures through genetic manipulation Domestication of plants via micropropagation micropropagation. Drug production Is the designing of transgenic plants to grow under specific environments in the presence (or absence) of chemicals. Pharmagenomics Gene therapy One hope is that green biotechnology might produce more environmentally friendly solutions than traditional industrial agriculture. i l Classification of Biotechnology White Biotechnology Blue Biotechnology also known as industrial biotechnology, is biotechnology applied to industrial processes. is a term that has been used to describe the marine and aquatic applications of biotechnology, but its use is relatively rare. Designing of an organism to produce a useful chemical. Using of enzymes as industrial catalysts to either produce valuable chemicals or destroy hazardous/polluting chemicals. Biotechnology vs. chemical processes Advandages of a biotechnological process - Using of highly active, specific and selective enzyme - Reduction R d i off pollution ll i - Gentle process conditions (p,T, c) - ATP as energy source - Using U i off cheap h raw materials t i l ((waste t products) d t ) -Biocompatibility of the products Disadvantage of a biotechnological Process -Low efficiency (accumulated needs in process development) - Low L concentrations t ti off th the products d t -Genetic instability of the biocatalysts or MO-strains -Process stability - High Investments for plants and education - High complexity and sensitivity of the processes - Low acceptance in the population Applications 1. Single Cell Proteins (SCP) 2. Metabolic products • • • • • 3. Productivity • • • • • Bioconversion Wastewater treatment Waste air treatment C Composting ti Metal production Alcohols Al h l Citric acid, Lactic acid Amino acids Vitamins Nucleotids 4. Active pharmaceutical ingredients • Erythopoetin • Insulin Nucleic acid - structure and organization Deoxyribonucleic acid (DNA) is a nucleic acid that contains the genetic instructions used in the development and functioning of all known living organisms with the exception of some viruses. DNA replication replication, the basis for biological inheritance, is a fundamental process occurring in all living organisms to copy their DNA. This process is „replication" in that each strand of th original the i i l double-stranded d bl t d d DNA molecule l l serves as template for the reproduction of the complementary strand. Transcription T i ti is i the th process off creating ti an equivalent RNA copy of a sequence of DNA. In translation, mRNA is decoded to produce a specific polypeptide. This polypeptide has the amino acid sequence specified by the DNA. The polypeptide is either the whole protein, or a part of it. Chemical structure of DNA DNA consists of two long polymers of simple units called nucleotides, with backbones made of sugars and phosphate groups joined by ester bonds bonds. These two strands run in opposite directions to each other and are therefore anti-parallel. Attached to each sugar is one of four types of molecules called bases. The backbone of the DNA strand is made from alternating phosphate and sugar residues. The sugar in DNA is 2-deoxyribose, which is a pentose (five-carbon) p ( ) sugar. g The sugars g are jjoined together by phosphate groups that form phosphodiester bonds between the third and fifth carbon atoms of adjacent sugar rings. Th strands The t d are antiparallel. ti ll l Chemical structure of DNA The asymmetric ends of DNA strands are called the 5` (five prime) and 3` (three prime) ends, with th 5' end the d having h i a terminal t i l phosphate h h t group and the 3' end a terminal hydroxyl group The DNA double helix is stabilized by hydrogen bonds between the bases attached to the two strands. The four bases found in DNA are adenine (A), (A) cytosine (C), guanine (G) and thymine (T). These four bases are attached to the sugar/phosphate to form the complete nucleotide. Chemical structure of DNA RNA Each nucleotide in RNA contains a ribose sugar, with carbons numbered 1' through 5'. A base is attached to the 1' position, generally adenine (A), cytosine (C), guanine (G) or uracile il (U). (U) Messenger RNA (mRNA) carries information about a protein sequence to the ribosomes ribosomes, the protein synthesis factories in the cell. It is codes so that every three nucleotides (a codon) correspond to one amino acid acid. Transfer RNA ((tRNA)) is a small RNA chain of about 80 nucleotides that transfers a specific amino acid to a growing polypeptide chain at the ribosomal site of protein synthesis y during g translation. It has sites for amino acid attachment and an anticodon region for codon recognition that binds to a specific sequence on the messenger RNA chain through hydrogen bonding. RNA-Functions Ribosomal RNA Ribosomal RNA (rRNA) is the catalytic component of the ribosomes. Eukaryotic ribosomes contain four different rRNA molecules: 18S 18S, 5 5.8S, 8S 28S and 5S rRNA. Three of the rRNA molecules are synthesized in the nucleolus, nucleolus and one is synthesized elsewhere . Ribosome Organization of the human Genome The haploid human genome contains ca. 23,000 protein-coding genes, far fewer than had been expected before its sequencing. In fact, only about 1.5% of the genome codes for proteins proteins, while the rest consists of non non-coding coding RNA genes genes, regulatory sequences, introns, and (controversially named) „junk „ DNA. Surprisingly, the number of human genes seems to be less than a factor of two greater than that of many much simpler organisms, such as the roundworm and the fruit fly fly. Genome Sizes Splicing Splicing However, human cells make extensive use of alternative splicing to produce several different proteins from a single gene, and the human proteome is thought to be much larger than those of the aforementioned organisms organisms. Biological function of proteins A graphical representation of the normal human karyotype DNA - packing of chromosoms Schema of protein biosynthesis DNA Replication DNA replication, the basis for biological inheritance, is a fundamental process occurring in all living organisms to copy their DNA DNA. This process is „replication" in that each strand of the original double-stranded DNA molecule serves as template for the reproduction of the complementary strand. In a cell, DNA replication begins at specific locations in the genome, called „origins". Unwinding of DNA at the origin, and synthesis of new strands, forms a replication fork. In addition to DNA polymerase, the enzyme that synthesizes the g nucleotides matched to the template p strand,, a number of new DNA byy adding other proteins are associated with the fork and assist in the initiation and continuation of DNA synthesis. Helicases are a class of enzymes vital to all living organisms. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands (i.e., DNA, RNA, or RNA-DNA hybrid) using energy derived from ATP hydrolysis. DNA-Replication Transcription During transcription, a DNA sequence is read by RNA polymerase, which produces a complementary, antiparallel RNA strand. As opposed to DNA replication, transcription results in an RNA complement that includes uracil (U) in all instances where thymine (T) would have occurred in a DNA complement. complement Transcription is the first step leading to gene expression. If the g gene transcribed encodes for a p protein,, the result of transcription p is messenger RNA (mRNA), which will then be used to create that protein via the process of translation. Alternatively, the transcribed gene may encode for either ribosomal RNA (rRNA) or transfer RNA (tRNA), tRNA), other components of the protein-assembly process, or other ribozmes. Transcription In eukaryotes, RNA polymerase, and therefore the initiation of transcription, requires the presence of a core promotor sequence in the DNA. Promoters are regions of DNA which promote transcription and in eukaryotes, are found at -30, -30 -75 and -90 base pairs upstream from the start site of transcription. Core promoters are sequences within the promoter which are essential for transcription initiation. RNA polymerase is able to bind to core promoters in the presence of various specific transkription factors. The most common type of core promoter in eukaryotes is a short DNA sequence known as a TATA box, found -30 base pairs from the start site of transcription. The TATA box, as a core promoter, is the binding site for a transcription factor known as TATA binding protein (TBP), which is itself a subunit of another transcription factor, called Transcription factor II D (TFIID). Initiation-Elongation-Termination Polymerase) (RNAP RNA Splicing In molecular biology, splicing is a modification of an RNA after transcription in which introns are removed and exons are joined transcription, joined. This is needed for the typical eukaryotic messenger RNA before it can be used to produce a correct protein through translation translation. For many eukaryotic introns, splicing is done in a series of reactions which are catalyzed by the spliceosome, a complex of small nuclear ribonucleoproteins (snRNPs), but there are also self-splicing introns. Alternative Splicing Splicing Translation Translation is the third stage of protein biosynthesis (part of the overall process of gene expression). In translation, messenger RNA (mRNA) produced by transcription is decoded by the ribosome to produce a specific amino acid chain chain, or poypeptide poypeptide, that will later fold into an active protein. Translation occurs in the cell cell's s cytoplasma, where the large and small subunits of the ribosome are located, and bind to the mRNA. g by y inducing g the binding g of tRNAs with The ribosome facilitates decoding complementary anticodon sequences to that of the mRNA. The tRNAs carry specific amino acids that are chained together into a polypeptide as the mRNA passes through and is "read" by the ribosome in a fashion reminiscent to that of a stock ticker and ticker tape. Translation Protein functions Antibodies - are specialized proteins involved in defending the body from antigens (foreign invaders) invaders). One way antibodies destroy antigens is by immobilizing them so that they can be destroyed by white blood cells. Contractile C il Proteins P i - are responsible ibl ffor movement. E Examples l iinclude l d actin i and myosin. These proteins are involved in muscle contraction and movement. Enzymes - are proteins that facilitate biochemical reactions. They are often referred to as catalysts because they speed up chemical reactions. Examples include the enzymes lactase and pepsin. Lactase breaks down the sugar lactose found in milk. Pepsin is a digestive enzyme that works in the stomach to break down proteins in food. Protein functions Hormonal Proteins - are messenger proteins which help to coordinate certain bodily activities activities. Examples include insulin insulin, oxytocin oxytocin, and somatotropin somatotropin. Insulin regulates glucose metabolism by controlling the blood-sugar concentration. Oxytocin stimulates contractions in females during childbirth. Somatotropin is a growth hormone that stimulates protein production in muscle cells cells. Structural Proteins - are fibrous and stringy and provide support. Examples include keratin, collagen, and elastin. Keratins strengthen protective coverings such as hair, quills, feathers, horns, and beaks. Collagens and elastin provide pp for connective tissues such as tendons and ligaments. g support Storage Proteins - store amino acids. Examples include ovalbumin and casein. Ovalbumin is found in egg whites and casein is a milk-based protein. Protein functions Transport Proteins - are carrier proteins which move molecules from one place to another around the body body. Examples include hemoglobin and cytochromes cytochromes. Hemoglobin transports oxygen through the blood. Cytochromes operate in the electron transport chain as electron carrier proteins. Amino acids Amino acids Abbreviation for Amino acids Peptide bond Protein amino acids are combined into a single polypeptide chain in a condensation reaction This reaction is catalysed by the reaction. ribosome in a process known as translation. The amino acids in a polymer are joined together by the peptide bonds between the carboxyl and amino groups of adjacent amino acid resid residues. es In general, the genetic code specifies 20 standard L- amino acids;; however,, in certain organisms the genetic code can include selenocysteine—and in certain archaea-pyrrolysine. Protein structures Primary structure: the amino acid sequence. Secondary structure: regularly repeating local structures stabilized by hydrogen bonds. The most common examples are the alpha helix, beta sheet and turns. Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a hydrophopic core, but also through salt bridges, hydrogen bonds, disulfide bonds, and even posttranslational modifications. Quaternary structure: the structure formed by several protein molecules (polypeptide chains), chains) usually called protein subunits subunits. Protein structures Protein modifications After translation, the posttranslational modification of amino acids extends the range of functions of the protein by attaching to it other biochemical functional groups g p such as acetate, phosphate, various lipids and carbohydrates, by changing the chemical nature of an amino acid (e.g. citrullination) or by making structural changes, like the formation of disulfide bridges. Protein - Modifications Der genetische Code The genetic code is the set of rules by which information encoded in genetic material (DNA ormRNA sequences) is translated into proteins (amino acid sequences) by living cells. The code defines a mapping between tri-nucleotide sequences, called codons,, and amino acids. With some exceptions, a triplet codon in a nucleic acid sequence specifies a single amino acid. acid There are 4³ 4 = 64 different codon combinations possible with a triplet codon of three nucleotides; all 64 codons are assigned for either amino acids or stop signals during translation. Genetic code The genetic code Enzyms Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions. In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, called the products. products Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few g many yp possibilities,, the set of enzymes y made in a cell reactions from among determines which metabolic pathways occur in that cell. Like all catalysts, enzymes work by lowering the activation energy for a reaction, thus dramatically increasing the rate of the reaction. As a result, products are formed faster and reactions reach their equilibrium state more rapidly. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions. Carbonic anhydrases reaction Inhibition Faktoren der Enzymaktivität Competitive inhibition In competitive inhibition, the inhibitor and substrate compete for the enzyme (i e they can not bind at the same time) (i.e., time). Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, methotrexate is a competitive inhibitor of the enzyme dihydrofolate reductase, which catalyzes the reduction of dihydrofolate to tetrahydrofolat tetrahydrofolat. Note that binding of the inhibitor need not be to the substrate binding site (as frequently stated), if binding of the inhibitor changes the conformation of the enzyme to prevent substrate binding and vice versa. p inhibition the maximal velocity y of the reaction is not changed, g , but In competitive higher substrate concentrations are required to reach a given velocity, increasing the apparent Km. Kinetics Uncompetitive inhibition and Non-competitive inhibition Uncompetitive inhibition In uncompetitive inhibition the inhibitor can not bind to the free enzyme, enzyme but only to the ES-complex. The EIS-complex thus formed is enzymatically inactive. This type of inhibition is rare, but may occur in multimeric enzymes. Non-competitive inhibition Non competitive inhibitors can bind to the enzyme at the same time as the Non-competitive substrate, i.e. they never bind to the active site. Both the EI and EIS complexes are enzymatically inactive. Because the inhibitor can not be driven from the enzyme by higher substrate concentration (in contrast to competitive inhibition), the apparent Vmax changes. But because the substrate can still bind to the enzyme, the Km stays the same. Enzyme classification EC 1 Oxidoreductases: catalyze oxidation/reduction reactions EC 2 T Transferases: f t transfer f a functional f ti l group (e.g. ( a methyl th l or phosphate group) EC 3 Hydrolases: catalyse the hydrolysis of various bonds EC 4 Lyases: y cleave various bonds by y means other than hydrolysis y y and oxidation EC5 Isomerases: catalyze isomerization changes within a single molecule EC6 Ligases: join two molecules with covalent bonds Industrial applications Phylogenetic tree of life Prokaryotic cell structure Eukaryotic cell structure Animal cell structure Centrioles - Centrioles are self-replicating organelles made up of nine bundles of microtubules and are found only in animal cells. They appear to help in organizing cell division, division but aren aren'tt essential to the process. process Cilia and Flagella - For single-celled eukaryotes eukaryotes, cilia and flagella are essential for the locomotion of individual organisms. In multicellular organisms, cilia function to move fluid or materials past an immobile cell as well as moving a cell or group of cells. Endoplasmic Reticulum - The endoplasmic reticulum is a network of sacs that manufactures, processes, and transports chemical compounds for use inside and outside of the cell. It is connected to the double-layered nuclear envelope, providing a pipeline between the nucleus and the cytoplasm. Animal cell structure Endosomes and Endocytosis - Endosomes are membrane-bound vesicles, formed via a complex family of processes collectively known as endocytosis, and found in the cytoplasm of virtually every animal cell cell. The basic mechanism of endocytosis is the reverse of what occurs during exocytosis or cellular secretion. It involves the invagination (folding inward) of a cell's plasma membrane to surround macromolecules or other matter diffusing through the extracellular fluid fluid. Golgi Apparatus - The Golgi apparatus is the distribution and shipping department for the cell's chemical products. It modifies proteins and fats built in the endoplasmic p reticulum and p prepares p them for export p to the outside of the cell. Animal cell structure Intermediate Filaments - Intermediate filaments are a very broad class of fibrous proteins that play an important role as both structural and functional elements of the cytoskeleton. Ranging in size from 8 to 12 nanometers, intermediate filaments function as tension-bearing elements to help maintain cell shape and rigidity. Lysosomes - The main function of these microbodies is digestion. Lysosomes break down cellular waste products and debris from outside the cell into simple p compounds, p , which are transferred to the cytoplasm y p as new cellbuilding materials. Animal cell structure Microfilaments - Microfilaments are solid rods made of globular proteins called actin These filaments are primarily structural in function and are an actin. important component of the cytoskeleton. Microtubules - These straight, straight hollow cylinders are found throughout the cytoplasm of all eukaryotic cells (prokaryotes don't have them) and carry out a variety of functions, ranging from transport to structural support. Mitochondria - Mitochondria are oblong shaped organelles that are found in the cytoplasm of every eukaryotic cell. In the animal cell, they are the main power generators,, converting g g oxygen yg and nutrients into energy. gy Nucleus - The nucleus is a highly specialized organelle that serves as the information p processing g and administrative center of the cell. This organelle g has two major functions: it stores the cell's hereditary material, or DNA, and it coordinates the cell's activities, which include growth, intermediary metabolism, protein synthesis, and reproduction (cell division). Animal cell structure Peroxisomes - Microbodies are a diverse group of organelles that are found in the cytoplasm, roughly spherical and bound by a single membrane. There are several types of microbodies but peroxisomes are the most common common. Plasma Membrane - All living cells have a plasma membrane that encloses their contents In prokaryotes, contents. prokaryotes the membrane is the inner layer of protection surrounded by a rigid cell wall. Eukaryotic animal cells have only the membrane to contain and protect their contents. These membranes also regulate the passage of molecules in and out of the cells. Ribosomes - All living cells contain ribosomes, tiny organelles composed of pp y 60 p percent RNA and 40 p percent p protein. In eukaryotes, y , ribosomes approximately are made of four strands of RNA. In prokaryotes, they consist of three strands of RNA Gram positive/Gram negative Plasmid A plasmid is a DNA molecule that is separate from, and can replicate independently of, the chromosomal DNA. They are double stranded and, in many cases, circular. Plasmids usually occur naturally in bacteria, but are sometimes found in eukaryotic organisms (e (e.g., g the 2-micrometre-ring in Saccharomyces cerevisiae) cerevisiae). Plasmid size varies from 1 to over 1,000kilobase pairs (kbp). The number of identical plasmids within a single cell can range anywhere from one to even thousands under some circumstances. part of the mobilome,, since they y are often Plasmids can be considered to be p associated with conjugation, a mechanism of horizontal gene transfer Plasmids used in genetic engineering are called vectors. Plasmids serve as important tools in genetics and biotechnology labs, where they are commonly used to multiply (make many copies of) or express particular genes. Bacterial DNA and plasmids Bacterial morphology Bacterial growth curve Bacterial growth Bacterial growth in batch culture can be modeled with four different phases: lag phase (A), exponential or log phase (B), stationary phase (C), and death phase (D). During lag phase, bacteria adapt themselves to growth conditions. It is the period where the individual bacteria are maturing and not yet able to divide. During the lag phase of the bacterial growth cycle, synthesis of RNA, enzymes and other molecules occurs. So in this phase the microorganisms are not dormant. Bacterial growth Exponential phase (sometimes called the log phase or the logarithmic phase) is a period characterized by cell doubling. The number of new bacteria appearing per unit time is proportional to the present population. population If growth is not limited, doubling will continue at a constant rate so both the number of cells and the rate of population increase doubles with each consecutive time period. period During stationary phase, the growth rate slows as a result of nutrient depletion and accumulation of toxic products. This phase is reached as the bacteria begin to exhaust the resources that are available to them. This phase is a constant value as the rate of bacterial growth is equal to the rate of bacterial death. At death phase, bacteria run out of nutrients and die. Autotroph An autotroph, or producer, is an organism that produces complex organiccompounds (such as carbohydrates, fats, and proteins) from simple inorganic molecules using energy from light (by photosynthesis) or inorganic chemical reactions (chemosynthesis). They are the producers in a food chain, such as plants on land or algae in water. They are able to make their own food and can fix carbon. g compounds p as an energy gy source or a carbon Therefore,, theyy do not use organic source. Autotrophs can reduce carbon dioxide (add hydrogen to it) to make organic compounds. An autotroph converts physical energy from sun light (in case of green plants) into chemical energy in the form of reduced carbon. Autotroph Autotrophs can be phototrophs or lithotrophs (chemoautotrophs). Phototrophs use light as an energy source, while lithotrophs oxidize inorganic compounds such as hydrogen sulfide compounds, sulfide, elemental sulfur sulfur, ammonium and ferrous iron. Phototrophs and lithotrophs use a portion of the ATP produced during photosynthesis or the oxidation of inorganic compounds to reduce NADP+ to g compounds. p NADPH in order to form organic Heterotrophs Heterotrophs, take in autotrophs as food to carry out functions necessary for their life Thus life. Thus, heterotrophs — all animals animals, almost all fungi fungi, as well as most bacteria and protozoa — depend on autotrophs for the energy and raw materials they need. Heterotrophs obtain energy by breaking down organic molecules (carbohydrates, fats, and proteins) obtained in food. Overview of cycle between autotrophs and heterotrophs Bacteria Bacteria are a large domain of single-cell, prokaryote microorganisms. Typically a few micrometers in length, bacteria have a wide range of shapes, ranging from p to rods and spirals p spheres Fungus A fungus is a member of a large group of eukaryotic organisms that includes g such as yyeasts and molds,, as well as the more familiar microorganisms mushrooms. Fungus Cells The range of sizes Biotech-Products Biotech-Products Biotech Products Catabolism Catabolism is the metabolic reaction cells undergo g to extract energy. gy There are two major metabolic pathways of monosaccharide catabolism: glycolysis and the citric acid cycle. Anabolic processes produce peptides, proteins, t i polysaccharides, l h id lilipids, id and d nucleic acid. Catabolism, the opposite of anabolism, produces smaller molecules used by the cell to synthesize larger molecules ATP und NADH ATP is consumed in the cell by energy-requiring (endothermic) processes and can be generated by energy-releasing (exothermic) processes. In this way ATP transfers energy energ between bet een spatiall spatially-separate separate metabolic reactions reactions. ATP is the main energy source for the majority of cellular functions. This includes the synthesis of macromolecules, including DNA and RNA (see below), and proteins. ATP also plays a critical role in the transport of macromolecules across cell membranes membranes, e.g. exocytosis and endocytosis. ATP iis consumed d iin th the cell ll by b energy-requiring i i (endothermic) ( d th i ) processes andd can be b generated t d by b energy-releasing (exothermic) processes. In this way ATP transfers energy between spatially-separate metabolic reactions. ATP is the main energy source for the majority of cellular functions. This includes the synthesis y of macromolecules,, includingg DNA and RNA,, and pproteins. ATP also pplays y a critical role in the transport of macromolecules across cell membranes, e.g. exocytosis and endocytosis. Adenosintriphosphat 8 kcal/mol ATP consists of adenosin — composed of an adenine ring and a ribose sugar — and three phosphate groups (triphosphate). The phosphoryl groups, starting with the group closest to the ribose, are referred to as the alpha (α), beta (β), and gamma (γ) phosphates.. ATP + H2O → ADP + Pi ∆G˚ = −30.5 kJ/mol (−7.3 kcal/mol) ATP + H2O → AMP + PPi ∆G˚ = −45.6 kJ/mol (−10.9 kcal/mol) Stoffwechselwege Metabolismus Glycolysis Glycolysis Glycolysis is the metabolic pathway that converts glucose C6H12O6, into pyruvate CH3COCOO− + H+. pyruvate, The free energy released in this process is used to form the high-energy compounds ATP (adenosine triphosphat) and NADH (reduced nicotinamide adenine dinucleotide). Entner-Doudoroff-Pathway Entner–Doudoroff pathway The Entner–Doudoroff pathway describes an alternate series of reactions that catabolize glucose to pyruvate using a set of enzymes different from those used in either glycoloysis or the pentose phosphat pathway. Most bacteria use glycolysis and the pentose phosphate pathway pathway. Citrat acid cycle Citrat acid cycle In aerobic organisms, the citric acid cycle is part of a metabolic pathway involved in the chemical conversion of carbohydrates carbohydrates, fats and proteins into carbon dioxide and water to generate a form of usable energy. Other relevant reactions in the pathway include those in glycolysis and pyruvat oxidation before the citric acid cycle, and oxidative phosphorylation after it. In addition, it provides precursors for many compounds including some amino performing g fermentation. acids and is therefore functional even in cells p Signal transduction Signal transduction is the process by which an extracellular signaling molecule activates a membrane receptor, that in turn alters intracellular molecules creating a response response. There are two stages in this process: 1) a signalling molecule activates a certain receptor on the cell membrane 2) causing a second messenger to continue the signal into the cell and elicit a physiological response. p, the signal g can be amplified, p , meaning g that one signalling g g molecule In either step, can cause many responses. Signaling pathways Signaling pathways EGF Pathway