To which major group of biomolecules does an enzyme belong?
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Proteins, amino acids.
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So many questions zapped in one, eh?\n\nOk, let me answer them one by one. First let us talk about Enzymes in general.\n\n1] Enzymes-\n\nStructures.\nThe enzymes can have different structures as there are too many functionally and structurally different enzymes. You can view and study the structures from the online Enzyme Structure Database. Here is the link-\nhttp://www.biochem.ucl.ac.uk/bsm/enzymes/\nhttp://www.cartage.org.lb/en/themes/sciences/lifescience/GeneralBiology/Biochemistry/Enzymes/Classification/Classification.htm\nFor further such web-pages, refer to the links listed here-\nhttp://www.google.com/search?hl=en&lr=&q=enzymes+structure&btnG=Search\n\nMode of Working.\nThe enzymes usually work by the "Lock and key" mechanism. They recognise the substrate and attatch to them. Thereafter, they change the substrate to the product and release it and remain unchanged in the process.\n\nHere are links with pictures and graphs that you might find useful-\nhttp://www.biologycorner.com/bio3/notes-enzymes.html\n\nLatest Research-\n1] http://www.sciencepages.co.uk/keystage4/GCSEChemistry/enzymeslinks.php\n2] http://www.google.com/search?hl=en&lr=&q=enzymes+research&btnG=Search\n3] http://www.musclemass.com/digestive_enzymes.html\n4] http://www.valleyenzymes.com/\n\n=========== ============ ============\n\n2- Amylases\n\nStructure\nTheir structures can also be found in the database here-\nhttp://www.biochem.ucl.ac.uk/bsm/enzymes/ as they are also enzymes. Here are a few more links that you might find useful-\n1] http://content.febsjournal.org/cgi/content/abstract/269/2/397\n2] http://www.google.com/search?hl=en&q=amylases+structure&btnG=Google+Search\n3] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=4196183&dopt=Abstract\n\nMode of action.\nSimilar to Enzymes. Here are a few more useful links-\n1] http://www.google.com/search?hl=en&q=amylases+working&btnG=Google+Search\n2] http://www.classofoods.com/page1_4.html\n3] http://www.realbeer.com/jjpalmer/ch14.html\n\nLatest Research.\n1] http://www.findarticles.com/p/search?tb=art&qt=Amylases+%2F+Research\n2] http://www.google.com/search?hl=en&q=amylases+research&btnG=Google+Search\n3] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=13835834&dopt=Abstract\n\n========= =========== ============\n\n3- Glucoamylases\n\nStructures.\nSee the database again-\nhttp://www.biochem.ucl.ac.uk/bsm/enzymes/\n\nA few more specific links are-\n1] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10491121&dopt=Abstract\n2] http://peds.oxfordjournals.org/cgi/content/abstract/7/3/393\n3] http://www.public.iastate.edu/~pedro/papers/coutinho94a.html\n4] http://www-hasylab.desy.de/science/annual_reports/2005_report/part2/contrib/72/14454.pdf  \n5] http://www.google.com/search?hl=en&q=glucoamylases+structure&btnG=Google+Search\n\nMode of Action\nSee Enzymes again. Some more specific links can be found here-\nhttp://www.google.com/search?hl=en&q=glucoamylases+working&btnG=Google+Search\n\nResearch.\nHere are some awesome pages-\n1] http://www.enzymestuff.com/conditionceliac.htm\n2] http://www.chemweb.com/journals?type=issue&jid=07349750&iid=00240001\n3] http://www.google.com/search?hl=en&q=glucoamylases+research&btnG=Google+Search\n4] http://www.bb.iastate.edu/FacultyResearchFolder/Robyt/Research.html\n5] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10767433&dopt=Abstract\n6] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2116499&dopt=Abstract
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Monosaccharide- \n\nMonosaccharides have single carbohydrate unit. They can have three or more carbon atoms. Classified as triose, tetrose, pentose, hexose ........ based on their carbon number.\nTriose-Glyceraldehyde\nTetrose- Erythrose\nPentose- Ribose, Ribulose\nHexose-Glucose, Fructose, Galactose, Mannose\n\nDisaccharide-\n\nTwo disaccharide loses a molecule of water to condense and form a disaccharide. \nExample- Sucrose, Celobiose\n\nPolysaccharide-\n\nCondensation polymer of monosaccharide units.\nExmp- Amylose, Cellulose, Glycogen
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Biochemistry focuses primarily on enzyme catalyzed and controlled chemical reactions.  Untimately, it is the study of all chemical processes endemic to life, but in practice this means that they focus primarily on the large proteins that serve to control and quicken biological chemical pathways.  They look at the way that chemical cascades are triggered or halted by looking that the interactions between proteins and the various substrates they work on.\n\nBroadly, we refer to biochemical pathways as metabolism.  This involves both catabolism (breaking down chemicals for energy, nutrients, or detoxification) and anabolism (the building of proteins to serve functions in the body--think "anabolic steroids," which make the body build excessive muscle protein.  "Anabolic" refers to the fact muscle growth is part of anabolism).
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here're some informative links http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Enzymes.html , http://en.wikipedia.org/wiki/Enzyme\n\nhope this helps.
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I'll give some examples and some brief explanations right here:\n\nSubstrate = A substrate is a compound that binds to an enzyme and is converted to a product.  In other words, a substrate is something an enzyme digests.  Anything that is digested is the substrate.\n\nEnzyme = Enzymes are globular proteins, larger in size compared to their substrates.  In other words, they are made up of proteins and digests substrates.\n\nNow, enzymes are 'digesters' and one kind of enzyme can only bind to one kind of substrate.  (e.g. Enzyme A can only bind to Substrate A and not Substrate B)   \n\nLactose = substrate\nLactase = enzyme\n\nHow do I know???\n\nMost substrates have an 'O' to replace the 'A' in Enzymes.\n\nNow, what happens after the enzymes bind/digest to the substrate?\n\nIt converts the substrate into smaller products.  In the Maltose case, maltOse gets digested by maltAse into glucose.  So, glucose in the final product\n\nillustrated by:\n\n``````````(is digested by)\n``````````````Maltase\nMaltose    ---------------->  Glucose\n(substrate)``(enzyme)``(Product)\n\n\nAnother illustrated example:\n\nProtein as the substrate.\n\n````````(is digested by)\n```````````````Pepsin\nProtein      ------------------>  Peptones/Large Polypeptides\n(Substrate)  ```(Enzyme) ````````````````(Product)
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# Large molecules in biological systems namely proteins, nucleic acids, and polysaccharides.\nwww.whatislife.com/glossary.htm\n\n# large single chemical entities such as pieces of DNA or RNA.\nwww.biologylessons.sdsu.edu/classes/lab3/glossary.html\n\n# A macromolecule is a molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass.\nen.wikipedia.org/wiki/Macromolecule\n\nA macromolecule is a molecule with a large molecular mass, but generally the use of the term is restricted to polymers and molecules which structurally include polymers. [1]\n\nMany examples come from biology and in particular biochemistry. These include proteins, starches, lipids and nucleic acids (such as DNA), which are sometimes called "biomacromolecules" or biopolymers. Synthetic examples include plastics. The integral domains of crystals and metals, while composed of very large numbers of atoms joined by molecule-like bonds, are rarely referred to as "macromolecules."\n\nThe term macromolecule is also sometimes used to refer to aggregates of two or more macromolecules held together by intermolecular forces rather than by chemical "bonds". This usage is common in particular when the individual macromolecules involved aggregate or "assemble" spontaneously and rarely exist in isolation. Such an aggregate is more properly called a macromolecular complex. In such a context, individual macromolecules are often referred to as subunits (see e.g. protein subunit).\n\nSubstances that are composed of macromolecules often have unusual physical properties. The properties of liquid crystals and such elastomers as rubber are examples. Although too small to see, individual pieces of DNA in solution can be broken in two simply by suctioning the solution through an ordinary straw. This is not true of smaller molecules. The 1964 edition of Linus Pauling's College Chemistry asserted that DNA in nature is never longer than about 5000 base pairs. This is because biochemists were inadvertently and with perfect consistency breaking their samples into pieces. In fact, the DNA of chromosomes can be tens of millions of base pairs long.\n\nAnother common macromolecular property that does not characterize smaller molecules is the need for assistance in dissolving into solution. Many require salts or particular ions to dissolve in water. Proteins will denature if the solute concentration of their solution is too high or too low.
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An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\n\nWhile all enzymes have a biological role, some enzymes are used commercially for other purposes. Many household cleaners use enzymes to speed up chemical reactions ( e.g., breaking down protein or starch stains in clothes).\n\nMore than 5,000 enzymes are known. Typically the suffix -ase is added to the name of the substrate (e.g., lactase is the enzyme that catalyzes the cleavage of lactose) or the type of reaction (e.g., DNA polymerase catalyzes the formation of DNA polymers). However, this is not always the case, especially when enzymes modify multiple substrates. For this reason Enzyme Commission or EC numbers are used to classify enzymes based on the reactions they catalyze. Even this is not a perfect solution, as enzymes from different species or even very similar enzymes in the same species may have identical EC numbers.\nIn enzymes, as with other proteins, function is determined by structure. An enzyme can be:\n\n    * A monomeric protein, i.e., containing only one polypeptide chain, typically one hundred or more amino acids; or\n    * an oligomeric protein consisting of several polypeptide chains, different or identical, that act together as a unit.\n\nAs with any protein, each monomer is actually produced as a long, linear chain of amino acids, which folds in a particular fashion to produce a three-dimensional product. Individual monomers may then combine via non-covalent interactions to form a multimeric protein. Many enzymes can be unfolded or inactivated by heating, which destroys the three-dimensional structure of the protein.\n\nhttp://en.wikipedia.org/wiki/Enzyme#3D_Structure
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nucleus, cytoplasm and protoplasm ....
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DNA is a polymer. The monomer units of DNA are nucleotides, and the polymer is known as a "polynucleotide." Each nucleotide consists of a 5-carbon sugar (deoxyribose), a nitrogen containing base attached to the sugar, and a phosphate group. There are four different types of nucleotides found in DNA, differing only in the nitrogenous base. The four nucleotides are given one letter abbreviations as shorthand for the four bases. \n\nA is for adenine \nG is for guanine \nC is for cytosine \nT is for thymine \nThe DNA backbone is a polymer with an alternating sugar-phosphate sequence. The deoxyribose sugars are joined at both the 3'-hydroxyl and 5'-hydroxyl groups to phosphate groups in ester links, also known as "phosphodiester" bonds
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Carbohydrates are classified by their number of sugar units: monosaccharides (such as glucose and fructose), disaccharides (such as sucrose and lactose), oligosaccharides, and polysaccharides (such as starch, glycogen, and cellulose).
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All biological processes are catalyzed by enzymes (proteins). The tertiary structure of all proteins is affected by pH. Why? Because the hydrogen and ionic bonds that maintain the tertiary structure can be broken by extremes in Hydrogen and Hydroxyl ion concentration. pH measures this concentration.
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Enzymes with different structures that catalyze the same reactions are called isoenzymes.  There can be many isoenzymes for one enzyme.  For example, lactate dehydrogenase has 5 different fractions.  They are LD1, LD2, LD3, LD4, and LD5.  They are named for the migration patterns in electrophoresis (the fraction that migrates the furthest, or goes fastest, is 1, and the slowest is 5.  Each LD fraction has a different combination of 2 subunits, H and M.  LD1 is HHHH, LD3 is HMMM, and LD5 is MMMM.
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Do you mean the molecular composition or macroscopic composition? There would be too much to post here so I suggest you visit the following\n\nhttp://users.rcn.com/jkimball.ma.ultranet/BiologyPages/B/Blood.html#formation
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A decarboxylase is an enzyme that removes a carboxyl group by converting it to carbon dioxide.
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enzyme, biological catalyst. The term enzyme comes from zymosis, the Greek word for fermentation, a process accomplished by yeast cells and long known to the brewing industry, which occupied the attention of many 19th-century chemists.\n \n Louis Pasteur recognized in 1860 that enzymes were essential to fermentation but assumed that their catalytic action was inextricably linked with the structure and life of the yeast cell. Not until 1897 was it shown by German chemist Edward Büchner that cell-free extracts of yeast could ferment sugars to alcohol and carbon dioxide; Büchner denoted his preparation zymase. This important achievement was the first indication that enzymes could function independently of the cell.\n \n The first enzyme molecule to be isolated in pure crystalline form was urease, prepared from the jack bean in 1926 by American biochemist J. B. Sumner, who suggested, contrary to prevailing opinion, that the molecule was a protein. In the period from 1930 to 1936, pepsin, chymotrypsin, and trypsin were successfully crystallized; it was confirmed that the crystals were protein, and the protein nature of enzymes was thereby firmly established.\n \n Enzymatic Action\n \n Like all catalysts, enzymes accelerate the rates of reactions while experiencing no permanent chemical modification as a result of their participation. Enzymes can accelerate, often by several orders of magnitude, reactions that under the mild conditions of cellular concentrations, temperature, pH, and pressure would proceed imperceptibly (or not at all) in the absence of the enzyme. The efficiency of an enzyme's activity is often measured by the turnover rate, which measures the number of molecules of compound upon which the enzyme works per molecule of enzyme per second. Carbonic anhydrase, which removes carbon dioxide from the blood by binding it to water, has a turnover rate of 106. That means that one molecule of the enzyme can cause a million molecules of carbon dioxide to react in one second.\n \n Most enzymatic reactions occur within a relatively narrow temperature range (usually from about 30°C to 40°C), a feature that reflects their complexity as biological molecules. Each enzyme has an optimal range of pH for activity; for example, pepsin in the stomach has maximal reactivity under the extremely acid conditions of pH 1–3. Effective catalysis also depends crucially upon maintenance of the molecule's elaborate three-dimensional structure. Loss of structural integrity, which may result from such factors as changes in pH or high temperatures, almost always leads to a loss of enzymatic activity. An enzyme that has been so altered is said to be denatured \n \n Consonant with their role as biological catalysts, enzymes show considerable selectivity for the molecules upon which they act (called substrates). Most enzymes will react with only a small group of closely related chemical compounds; many demonstrate absolute specificity, having only one substrate molecule which is appropriate for reaction.\n \n Numerous enzymes require for efficient catalytic function the presence of additional atoms of small nonprotein molecules. These include coenzyme molecules, many of which only transiently associate with the enzyme. Nonprotein components tightly bound to the protein are called prosthetic groups. The region on the enzyme molecule in close proximity to where the catalytic event takes place is known as the active site. Prosthetic groups necessary for catalysis are usually located there, and it is the place where the substrate (and coenzymes, if any) bind just before reaction takes place.\n \n The side-chain groups of amino acid residues making up the enzyme molecule at or near the active site participate in the catalytic event. For example, in the enzyme trysin, its complex tertiary structure brings together a histidine residue from one section of the molecule with glycine and serine residues from another. The side chains of the residues i
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Wow... that's a question that could be answered on many different levels, and you're optimistic as hell to think you can get a "real" answer here. Basically, an enzyme provides a micro-enviroment that is very conducive to the formation of an intermediate form that leads from the substrate to the product. Another way of saying this is that an enzyme, like any other catalyst, lowers the activation energy of a reaction.\n\nBut seriously, dude. You're asking for a course in biochemistry here. Try Stryer, or any other classic biochem textbook, for a more thorough answer.