5.1.4.1. Nucleotide functions

Nucleotide functions

There are different nucleotides that participate in many biochemical processes, and may have these functions:

Nucleic acid precurors

Nucleic acid precursors, since, as we have seen, 5'-monophosphate nucleotides, ribonucleotides and deoxyribonucleotides, are the monomers of RNA and DNA.

Non-nucleic nucleotides

Other nucleotides are not part of nucleic acids, such as:

- Adenosine phosphates: ribonucleotides of adenine linked by phosphoester bonds one, two or three molecules of phosphoric acid, respectively:

AMP: Adenosine monophosphate (Adenine-Ribose-P).
ADP: Adenosindiphosphate (Adenine-Ribose-PP).
ATP: Adenosine triphosphate (Adenine-Ribose-PPP).

This phosphoester bond that is established between nucleotides is a high-energy, hydrolyzable bond, so they can act as energy transporters. The ATP is considered the universal unit of energy .

ADP, adenosine diphosphate, if it has energy at its disposal, uses it to join a third phosphate group to the other two to obtain adenosine triphosphate (ATP).

By derivative work: Batterytime (talk)ATP_structure.svg: User:Mysid (ATP_structure.svg) [Public domain], via Wikimedia Commons

To form this bond a lot of energy is needed (8 kcal / mol), and when it breaks, it will release the same amount of energy.

Although energy is not stored as such, energy used to form the bond and released later when the bond is broken by hydrolysis in exothermic reactions, makes ADP and ATP molecules considered energy carriers.

If there is a lot of energy available, many ATP molecules will be formed from ADP, so the ATP / ADP ratio will be high. If the amount of energy available to the cell is small, it will decrease ATP levels and increase those of ADP, so the ATP / ADP ratio will be lower.

The energy released in exergonic reactions is used to form ATP from ADP and phosphoric acid (phosphorylation), while the energy needed in endergonic reactions comes from that released when ATP is hydrolyzed to ADP and phosphoric acid (dephosphorylation).

Typically, the high-energy bonds that exist between phosphate groups are represented by the virgulilla symbol (~), rather than the usual notation (-) for bonds.

Other ATP- like ribonucleotides such as GTP, UTP, and CTP play a more limited role as energy transferors.

Coenzymes

The coenzymes are cofactors nonprotein organic, thermosetting, which attached to a apoenzyme form the holoenzyme, and generally act as electron carriers. Many of the coenzymes are nucleotides.

Unlike enzymes, coenzymes are not specific in terms of the substrate on which they act, but rather each group of coenzymes intervenes in the same type of reaction, regardless of the substrate.

Some enzymes catalyze oxidation and reduction reactions in the cell, in which the transfer of electrons occurs. If one enzyme is oxidized, another will simultaneously be reduced, and vice versa. These coenzymes are responsible for the transfer of these electrons, so they have two forms, reduced (represented with more hydrogens) and another oxidized.

Pyridin-nucleotides: consisting of a nucleotide nicotinamide (niacin derivative or vitamin B₃) and a ribonucleotide of adenine. Two oxidized forms are known:
- NAD⁺: nicotinamide-adenine-dinucleotide. Its reduced form is presented as NADH + H⁺.
- NADP⁺: nicotinamide-adenine-dinucleotide-phosphate (its formula is the same as that of NAD⁺, but it has a phosphate group on the 2' carbon of the adenine nucleotide) with two or three phosphoric acid molecules, respectively. Its reduced form is NADPH + H⁺.

The pyridine-nucleotides are coenzymes redox reactions acting as electron carriers, being the reduced forms NADH and NADPH. They are involved in various metabolic processes, such as cellular respiration.

By NAD_oxidation_reduction.svg: Fvasconcellos 19:44, 9 December 2007 (UTC). w:Image:NAD oxidation reduction.png by Tim Vickers.derivative work: Gustavocarra (NAD_oxidation_reduction.svg) [Public domain], via Wikimedia Commons

Flavin-nucleotides: they are derivatives of riboflavin (vitaminB₂), of which two oxidized forms are known:
- FMN: flavin-mononucleotide, which is a phosphoric acid molecule bound to riboflavin.
- FAD: flavin-adenine-dinucleotide, which is the former attached to an adenine nucleotide.

They also act as electron transporters in oxidation and reduction reactions, the reduced forms being FMNH₂ and FADH₂. To pass from one form to another, they capture or give up hydrogen by oxidizing or reducing the substrate.

They differ from pyridine nucleotides (nicotinamide coenzymes), in that flavin nucleotides are strongly bound to enzymes, which is why they are called prosthetic groups.

Coenzyme A: it is formed by pantothenic acid (vitamin of group B) joined to an ADP (adenosine-diphosphate). The active part of the molecule is a thiol group (radical –SH), that is why it is also represented as CoA-SH, and acts as a carrier for acetyl groups (two-carbon hydrocarbon chains) and acyl groups (“n” hydrocarbon chains carbons).

Chemical messengers

For example, cyclic adenosine monophosphate (cAMP), which originates when phosphate binds to the 3' and 5' carbons of ribose (two ester bonds) forming a cyclic phosphodiester bond.

The cAMP, cyclic adenosine monophosphate, is formed in cells from ATP, through a reaction catalyzed by the enzyme adenylate cyclase located in the cell membrane.

The cAMP acts as a mediator in many hormonal processes, transmitting and amplifying signals that reach the cells of hormones.

Fundamental Ideas About Nucleotide Functions

The main functions of nucleotides are:

Structural function: they are the constituents of nucleic acids.
Storage function and provide energy. When energy is obtained in a chemical reaction, an ADP molecule joins another phosphate group to form ATP through a high-energy bond. By breaking this link, energy will be obtained again.
Coenzyme function. They participate in cellular catabolism. Coenzymes take up H⁺ and electrons and remain as NADH, NADPH, and FADH₂, respectively. In the reduced state, they can easily give up H⁺ and electrons to other molecules.
Function of chemical messengers. The molecule of cyclic adenosine monophosphate (cAMP) is involved in many hormonal processes, transmitting and amplifying signals that reach the cells of hormones.

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BIOLOGÍA - GEOLOGÍA . COM
1st ESO	3rd ESO	4th ESO	Biology 2nd Baccalaureate
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Skip navigation Biology 2nd Baccalaureate Biology 2nd Bac. 1. Bioelements and biomolecules. Water and mineral salts 1.1. Chemical bonds in biology 1.1.1. Intramolecular bonds 1.1.1.1. Covalent bond 1.1.1.2. Ionic bond 1.1.2. Intermolecular bonds 1.1.2.1. Van der Waals forces 1.1.2.2. Hydrogen bonds 1.2. The chemical basis of life: inorganic and organic components 1.2.1. Primary bioelements 1.2.2. Secondary bioelements 1.2.3. Trace elements 1.3. The immediate principles or biomolecules 1.3.1. Water 1.3.1.1. Chemical structure of water 1.3.1.2. Properties and functions of water 1.3.2. Mineral salts 1.3.2.1. Functions of salts in solution 1.3.2.2. Colloidal solutions and dispersions 1.3.2.3. Properties of colloidal dispersions 1.3.2.4. Diffusion, osmosis and dialysis 1.3.2.4.1. Diffusion 1.3.2.4.2. Osmosis 1.3.2.4.3. Dialysis 1.4. Bibliography 2. Glucides 2.1. Glucid concept 2.2. Classification of carbohydrates 2.3. Monosaccharides 2.3.1. Trioses 2.3.1.1. Spatial isomerism or stereoisomerism 2.3.2. Tetroses 2.3.3. Pentoses 2.3.3.1. Monosaccharide cyclization 2.3.4. Hexoses 2.4. The N-glucosidic and O-glucosidic bonds 2.4.1. Substances derived from monosaccharides 2.5. Disaccharides 2.6. Polysaccharides 2.6.1. Homopolysaccharides 2.6.1.1. Reserve homopolysaccharides 2.6.1.2. Structural homopolysaccharides 2.6.2. Heteropolysaccharides 2.6.3. Heterosides 2.7. General functions of glucides 2.8. Bibliography 3. Lipids 3.1. Lipid concept 3.2. Classification of lipids 3.2.1. Fatty acids 3.2.1.1. Saturated and unsaturated fatty acids 3.2.1.2. Chemical properties of fatty acids 3.2.1.3. Physical properties of fatty acids 3.2.1.4. Fatty Acid Functions 3.2.2. Saponifiable lipids or with fatty acids 3.2.2.1. Simple lipids 3.2.2.1.1. Acylglycerides 3.2.2.1.2. Cerides 3.2.2.2. Complex lipids 3.2.2.2.1. Phospholipids 3.2.2.2.2. Glycolipids 3.2.3. Unsaponifiable lipids or without fatty acids 3.3. Lipid functions 3.4. Bibliography 4. Proteins 4.1. Introduction to proteins 4.2. Amino acids 4.2.1. Classification of amino acids 4.2.2. Properties of amino acids 4.3. The peptide bond 4.4. Protein 4.4.1. Protein structure 4.4.1.1. Primary structure of proteins 4.4.1.2. Secondary structure of proteins 4.4.1.3. Tertiary structure of proteins 4.4.1.4. Quaternary structure of proteins 4.4.2. Protein properties 4.4.3. Classification of proteins 4.4.3.1. Holoproteins 4.4.3.2. Heteroproteins 4.4.4. Protein functions 4.5. Enzymes 4.5.1. Structure of enzymes 4.5.2. The active center of enzymes 4.5.3. General Mechanism of Enzyme Catalysis 4.5.4. Regulation of enzyme activity 4.5.5. Allosteric enzymes 4.5.6. Nomenclature and classification of enzymes 4.6. The vitamins 4.6.1. Fat-soluble vitamins 4.6.2. Water soluble vitamins 4.7. Bibliography 5. Nucleotides and nucleic acids 5.1. The chemical composition of nucleic acids 5.1.1. Components of nucleic acids 5.1.2. Concept, types and functions of nucleic acids 5.1.3. Nucleosides 5.1.4. Nucleotides 5.1.4.1. Nucleotide functions 5.1.5. Nucleic acids 5.2. Deoxyribonucleic acid (DNA) 5.2.1. DNA structure 5.2.1.1. Primary structure of DNA 5.2.1.2. Secondary structure of DNA 5.2.1.3. Tertiary structure of DNA 5.2.1.3.1. Tertiary structure of DNA in prokaryotes 5.2.1.3.2. Tertiary structure of DNA in eukaryotes 5.2.1.4. Quaternary structure of DNA 5.2.2. DNA types 5.2.3. Genetic material: chromatin and chromosomes 5.2.3.1. Karyotype and karyogram 5.3. Ribonucleic acid (RNA) 5.3.1. RNA types 5.3.1.1. Transfer RNA 5.3.1.2. Messenger RNA 5.3.1.3. Ribosomal RNA 5.3.1.4. Nucleolar RNA 5.3.1.5. Small nuclear RNA 5.3.2. Functions of ribonucleic acids 5.4. Bibliography 6. Cell morphology 6.1. Cell concept 6.1.1. Cell history 6.1.2. Cell theory 6.2. Levels of cellular organization 6.2.1. General characteristics of cells 6.2.2. Prokaryotic cells 6.2.2.1. Prokaryotic cell morphology 6.2.2.2. Structure of prokaryotes 6.2.2.2.1. Bacterial capsule 6.2.2.2.2. Bacterial wall 6.2.2.2.3. Plasma membrane 6.2.2.2.4. Cytoplasm-Ribosomes-Inclusions 6.2.2.2.5. Bacterial DNA 6.2.2.2.6. Bacterial appendages 6.2.2.3. Bacteria Physiology 6.2.3. Eukaryotic cells 6.2.3.1. Animal and plant cell 6.2.3.1.1. Animal eukaryotic cell 6.2.3.1.2. Plant eukaryotic cell 6.2.3.2. Cell Evolution: Endosymbiont Theory 6.3. Size, shape and quantity 6.4. The plasma membrane 6.4.1. Chemical composition of the membrane 6.4.2. The structure of the membrane. The fluid mosaic model 6.4.3. Functions of the plasma membrane 6.4.4. Transport across the membrane 6.4.4.1. Small molecule transport 6.4.4.2. Macromolecule transport 6.4.5. Plasma membrane differentiations 6.5. The cell wall of plant cells 6.5.1. Chemical composition of the cell wall 6.5.2. Cell wall structure 6.5.3. Cell wall differentiations 6.5.4. Cell wall functions 6.6. Extracellular matrix or glucocalyx 6.7. Cytosol or hyaloplasm 6.8. The cytoskeleton 6.8.1. Microfilaments or actin filaments 6.8.2. Intermediate filaments 6.8.3. Microtubules 6.9. Cell membrane and organelle systems 6.9.1. Membrane systems 6.9.1.1. The endoplasmic reticulum 6.9.1.2. Golgi apparatus 6.9.2. Cell organelles 6.9.2.1. Lysosomes 6.9.2.2. Peroxisomes 6.9.2.3. Vacuoles 6.9.2.4. Mitochondria 6.9.2.4.1. Functions of the mitochondria 6.9.2.5. Plastids 6.9.2.5.1. Chloroplasts 6.9.2.6. Ribosomes 6.9.2.7. Centrosome 6.9.2.8. Cilia and flagella 6.10. Cell motility 6.11. The cell nucleus 6.11.1. Characteristics of the cell nucleus 6.11.2. The interphase nucleus 6.11.3. The mitotic nucleus or nucleus in division 6.12. Bibliography 7. Metabolism 7.1. Metabolism 7.1.1. Energetic Aspects of Cellular Chemical Reactions 7.2. Catabolism 7.2.1. Catabolism and obtaining energy 7.2.2. Carbohydrate catabolism 7.2.2.1. Glycolysis 7.2.2.2. Cellular respiration 7.2.2.2.1. Oxidative decarboxylation 7.2.2.2.2. Krebs cycle 7.2.2.2.3. Electron transport chain 7.2.2.2.4. Energy balance of cellular respiration 7.2.2.3. Fermentations 7.2.2.3.1. Alcoholic or ethyl fermentation 7.2.2.3.2. Lactic fermentation 7.2.2.3.3. Other types of fermentations 7.3. Anabolism 7.3.1. Autotrophic anabolism 7.3.2. Photosynthesis 7.3.2.1. Photochemical or light phase 7.3.2.1.1. Photosystems 7.3.2.1.2. Photophosphorylation 7.3.2.1.2.1. Non cyclic photophosphorylation 7.3.2.1.2.2. Cyclic photophosphorylation 7.3.2.2. Biosynthetic or dark phase 7.3.2.3. Factors influencing photosynthesis 7.3.2.4. Products of photosynthesis 7.3.3. Chemosynthesis 7.4. Bibliography 8. Cell reproduction 8.1. The cell cycle 8.1.1. Interphase 8.1.2. Cellular division 8.2. Cellular division 8.2.1. Mitosis 8.2.1.1. Prophase 8.2.1.2. Metaphase 8.2.1.3. Anaphase 8.2.1.4. Telophase 8.2.1.5. Cytokinesis 8.2.1.6. More on mitosis 8.2.2. Meiosis 8.2.2.1. Meiosis I 8.2.2.2. Meiosis II 8.2.3. Meiosis and sexual reproduction 8.2.4. Meiosis and life cycle 8.2.5. Biological importance of meiosis 8.3. Differences and similarities between mitosis and meiosis 8.4. Bibliography 9. Classical genetics 9.1. Genetics basics 9.2. Mendelian genetics 9.2.1. The method 9.2.2. Mendel's Laws 9.2.2.1. Mendel's first law or principle of uniformity in the first generation 9.2.2.2. Mendel's second law or principle of segregation 9.2.2.2.1. Backcross and test crossover 9.2.2.3. Mendel's third law or principle of independent combination 9.3. Gene interaction 9.3.1. Gene interaction between allelic genes 9.3.2. Gene interaction between non-allelic genes that influence for the same trait 9.4. Chromosomal theory of heredity 9.5. Ligation and recombination 9.6. Complex mendelism 9.6.1. Multiple allelism 9.6.1.1. Lethal genes 9.6.2. Pleiotropy 9.6.3. Expressiveness and genetic penetrance 9.7. Sex-linked inheritance 9.7.1. Y-linked inheritance 9.7.2. X-linked inheritance 9.8. Heredity influenced by sex 9.9. Bibliography 10. Molecular genetics 10.1. DNA as hereditary material 10.2. DNA replication 10.2.1. The need for DNA replication 10.2.2. First hypotheses about DNA duplication 10.2.3. Meselson and Stahl experiment 10.2.4. The sense of growth of the new strands 10.2.5. Mechanism of DNA replication 10.2.5.1. Replication in prokaryotes 10.2.5.2. Replication in eukaryotes 10.2.6. Error correction 10.2.7. Enzymes involved in replication 10.3. Gene concept 10.4. "One gene-one enzyme" theory 10.5. Transcription 10.5.1. Mechanism of transcription 10.5.1.1. Transcription in prokaryotes 10.5.1.2. Eukaryotic transcription 10.6. Translation or protein biosynthesis 10.6.1. The genetic code 10.6.2. Mechanism of translation of RNA to proteins 10.6.2.1. Translation in eukaryotes 10.7. Regulation of gene expression 10.8. Bibliography 11. Genetics and evolution 11.1. Mutations 11.2. Types of mutations 11.2.1. Gene or point mutation 11.2.2. Chromosomal or structural mutation 11.2.3. Mutation at the genomic level 11.3. Causes of mutations 11.4. Evolutionary implications of mutations 11.5. Metabolic implications of mutations 11.6. Bibliography 12. Microbiology and biotechnology 12.1. Microbiology 12.2. Viruses 12.2.1. Viral morphology 12.2.2. Viral physiology 12.2.2.1. Lytic cycle 12.2.2.2. Lysogenic cycle 12.2.2.3. Cycles of viruses of special interest 12.2.2.3.1. Flu virus life cycle 12.2.2.3.2. Life cycle of the AIDS virus 12.3. Other acellular forms 12.3.1. Viroids 12.3.2. Prions 12.4. Biotechnology 12.5. Bibliography 13. Immunology 13.1. Infection concept 13.2. Defense mechanisms against infections 13.2.1. Nonspecific mechanisms 13.2.1.1. Primary barriers: external defenses 13.2.1.2. Secondary barriers: internal defenses 13.2.2. Specific mechanisms 13.3. Immunity and immune system 13.3.1. Components of the immune system 13.3.2. Concept and nature of antigens 13.4. The immune response 13.4.1. Humoral immune response: the antibodies 13.4.1.1. Antibody-producing cells: B lymphocytes 13.4.1.2. Antibodies 13.4.1.2.1. Types of antibodies 13.4.1.2.2. Antigen-antibody reaction 13.4.1.3. Immune memory: primary and secondary responses 13.4.2. Cellular immune response: T lymphocytes 13.5. Types of immunity 13.5.1. Natural immunity 13.5.2. Artificial immunity 13.6. Immune system disorders 13.6.1. Autoimmunity 13.6.2. Hypersensitivity 13.6.3. Immunodeficiency 13.6.4. Transplants and the phenomenon of rejections 13.7. Bibliography « Previous \| Next » 5.1.4.1. Nucleotide functions Nucleotide functions There are different nucleotides that participate in many biochemical processes, and may have these functions: Structural function. Storage function and provide energy. Coenzyme function. Function of chemical messengers. Nucleic acid precurors Nucleic acid precursors, since, as we have seen, 5'-monophosphate nucleotides, ribonucleotides and deoxyribonucleotides, are the monomers of RNA and DNA. Non-nucleic nucleotides Other nucleotides are not part of nucleic acids, such as: - Adenosine phosphates: ribonucleotides of adenine linked by phosphoester bonds one, two or three molecules of phosphoric acid, respectively: AMP: Adenosine monophosphate (Adenine-Ribose-P). ADP: Adenosindiphosphate (Adenine-Ribose-PP). ATP: Adenosine triphosphate (Adenine-Ribose-PPP). This phosphoester bond that is established between nucleotides is a high-energy, hydrolyzable bond, so they can act as energy transporters. The ATP is considered the universal unit of energy . ADP, adenosine diphosphate, if it has energy at its disposal, uses it to join a third phosphate group to the other two to obtain adenosine triphosphate (ATP). By derivative work: Batterytime (talk)ATP_structure.svg: User:Mysid (ATP_structure.svg) [Public domain], via Wikimedia Commons To form this bond a lot of energy is needed (8 kcal / mol), and when it breaks, it will release the same amount of energy. Although energy is not stored as such, energy used to form the bond and released later when the bond is broken by hydrolysis in exothermic reactions, makes ADP and ATP molecules considered energy carriers. If there is a lot of energy available, many ATP molecules will be formed from ADP, so the ATP / ADP ratio will be high. If the amount of energy available to the cell is small, it will decrease ATP levels and increase those of ADP, so the ATP / ADP ratio will be lower. The energy released in exergonic reactions is used to form ATP from ADP and phosphoric acid (phosphorylation), while the energy needed in endergonic reactions comes from that released when ATP is hydrolyzed to ADP and phosphoric acid (dephosphorylation). Typically, the high-energy bonds that exist between phosphate groups are represented by the virgulilla symbol (~), rather than the usual notation (-) for bonds. Other ATP- like ribonucleotides such as GTP, UTP, and CTP play a more limited role as energy transferors. Coenzymes The coenzymes are cofactors nonprotein organic, thermosetting, which attached to a apoenzyme form the holoenzyme, and generally act as electron carriers. Many of the coenzymes are nucleotides. Unlike enzymes, coenzymes are not specific in terms of the substrate on which they act, but rather each group of coenzymes intervenes in the same type of reaction, regardless of the substrate. Some enzymes catalyze oxidation and reduction reactions in the cell, in which the transfer of electrons occurs. If one enzyme is oxidized, another will simultaneously be reduced, and vice versa. These coenzymes are responsible for the transfer of these electrons, so they have two forms, reduced (represented with more hydrogens) and another oxidized. Pyridin-nucleotides: consisting of a nucleotide nicotinamide (niacin derivative or vitamin B₃) and a ribonucleotide of adenine. Two oxidized forms are known: NAD⁺: nicotinamide-adenine-dinucleotide. Its reduced form is presented as NADH + H⁺. NADP⁺: nicotinamide-adenine-dinucleotide-phosphate (its formula is the same as that of NAD⁺, but it has a phosphate group on the 2' carbon of the adenine nucleotide) with two or three phosphoric acid molecules, respectively. Its reduced form is NADPH + H⁺. The pyridine-nucleotides are coenzymes redox reactions acting as electron carriers, being the reduced forms NADH and NADPH. They are involved in various metabolic processes, such as cellular respiration. By NAD_oxidation_reduction.svg: Fvasconcellos 19:44, 9 December 2007 (UTC). w:Image:NAD oxidation reduction.png by Tim Vickers.derivative work: Gustavocarra (NAD_oxidation_reduction.svg) [Public domain], via Wikimedia Commons Flavin-nucleotides: they are derivatives of riboflavin (vitaminB₂), of which two oxidized forms are known: FMN: flavin-mononucleotide, which is a phosphoric acid molecule bound to riboflavin. FAD: flavin-adenine-dinucleotide, which is the former attached to an adenine nucleotide. They also act as electron transporters in oxidation and reduction reactions, the reduced forms being FMNH₂ and FADH₂. To pass from one form to another, they capture or give up hydrogen by oxidizing or reducing the substrate. They differ from pyridine nucleotides (nicotinamide coenzymes), in that flavin nucleotides are strongly bound to enzymes, which is why they are called prosthetic groups. Coenzyme A: it is formed by pantothenic acid (vitamin of group B) joined to an ADP (adenosine-diphosphate). The active part of the molecule is a thiol group (radical –SH), that is why it is also represented as CoA-SH, and acts as a carrier for acetyl groups (two-carbon hydrocarbon chains) and acyl groups (“n” hydrocarbon chains carbons). Chemical messengers For example, cyclic adenosine monophosphate (cAMP), which originates when phosphate binds to the 3' and 5' carbons of ribose (two ester bonds) forming a cyclic phosphodiester bond. The cAMP, cyclic adenosine monophosphate, is formed in cells from ATP, through a reaction catalyzed by the enzyme adenylate cyclase located in the cell membrane. The cAMP acts as a mediator in many hormonal processes, transmitting and amplifying signals that reach the cells of hormones. Fundamental Ideas About Nucleotide Functions The main functions of nucleotides are: Structural function: they are the constituents of nucleic acids. Storage function and provide energy. When energy is obtained in a chemical reaction, an ADP molecule joins another phosphate group to form ATP through a high-energy bond. By breaking this link, energy will be obtained again. Coenzyme function. They participate in cellular catabolism. Coenzymes take up H⁺ and electrons and remain as NADH, NADPH, and FADH₂, respectively. In the reduced state, they can easily give up H⁺ and electrons to other molecules. Function of chemical messengers. The molecule of cyclic adenosine monophosphate (cAMP) is involved in many hormonal processes, transmitting and amplifying signals that reach the cells of hormones. Licensed under the Creative Commons Attribution Share Alike License 4.0 « Previous \| Next » These pages are semi-automatically translated from the web Biology 2nd Baccalaureate. Biología de 2º de Bachillerato (biologia-geologia.com). You can make any suggestion, question, comment, ..., in our forum 2º Bachillerato Biología - Foro de biologia-geologia.com
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Nucleotide functions

Nucleic acid precurors

Non-nucleic nucleotides

Coenzymes

Chemical messengers