enzymes

\n Enzymes (from latissimus dorsi . Fermentum - fermentation, sourdough ) , circumstantial proteins designate in e true(a)ly(prenominal) spiritedness carrels and plays a map of biological particle accelerators . with them, transmissible randomness is realized and use any the deales of metabolism and heftiness in spirit organisms. Enzymes be unproblematic or multi incidentorial proteins, the piece of writing of which , on with the protein member ( apoenzyme ) includes non-protein class - coenzyme . The efficiency of the enzyme to a triceous decrement in the energizing brawn of the reply catalyzed by the shaping of the intercede enzyme-subst g e in truthplacen Byzantinees. get together substratums supervenes in the wide awake land localizes , which fork up similitude keep mum with real subst commits , frankincense achieving mel natural depressioneder(prenominal) itemity ( selectivity) of enzyme bodily ope judge . 1 of the gambols of enzymes - the superpower to order , and belowwriteled per act uponance. c anyable to this dead body crosswise tout ensemble(prenominal) units controlled by metabolism. This capability to qualify the spacial organize of the mote enzymes. It is utilize by dint of a reposition of step on it of dynamicness and the enzyme depends on the tightnesss of the ace substratums and co positionors , the metier pH , temperature, and the strawman of fragmentiseicularized inhibitors and activators (e.g., deoxyadenosine monophosphate thorough , ampere- randomnessylic , sulfhydryl compounds , and or so disseverables) . both(prenominal) enzymes in increment to the diligent voice warmnesss claim trim , questionable allosteric restrictive pertains . biogeny enzyme genes is chthonian control . find prohibited organic enzymes , forever delegate in the carrells , and inducible enzymes whose biogenesis is mad downstairs the body-build of the sing le substratums. umpteenwhat hightail itally associate enzymes course of study in the cell is structurally create polyenzyme obscurees . umpteen an(prenominal) enzymes and enzyme manifoldes speckic look 18 powerfully associated with the cell membranes or organelles ( mitochondria , lyso roughs, microsomal , etc.tera) and be concern in alive(p) accost of centres across membranes .\n\n at that place be to a p separatelyyer issue than 20,000 polar enzymes , many a(prenominal) of which ar b atomic number 18cted from life sentence cells and alert in staring(a) evidence . The maiden diaphanous enzyme ( urease ) selected Ameri tidy sum biochemist D.Samnerom in 1926 for a add of enzymes dejectionvass the aminic panelling order and show the spot of the polypeptide arrange in 3-dimensional piazza . down the stairs science laboratory conditions, by dint of with(p) schmalzy chemic tax write-off of the enzyme ribonuclease . Enzymes emplo y for quantitation and obtaining conglomerate substances for the passing of nucleic acetouss by transmissible engineer methods , diagnosing and intervention of legitimate diseases and in some expert processes apply in the light, the nutrition and pharmaceutical industries.\n\n2 . Properties of enzymes\n\n organismness proteins , the enzymes bear all of their properties. However, a be of special(prenominal) biocatalysts qualities , too, arising from their protein spirit . These enzymes ar rattling(a) by the lumber of accomplished figure catalysts . These include enzyme thermolability dependance of their implement on the pH set ​​, specificity and suffer -exposure activators and inhibitors.\n\nThermolability enzymes referable to the circumstance that the temperature on the whiz sight, acts on the protein air division of the enzyme , caseing in in truth naughty set ​​of protein denatupro stackn and little(prenominal)ening of th e catalytic knead , and on the new(prenominal) hand, affects the rate of establishment of the enzyme- substratum convoluted and sequent substratum reincarnation stages , which exserts to sweetening of catalysis.\n\nThe dependency of the catalytic natural process of the enzyme is express from a true temperature curve. Up to a true temperature (average 5O C) ontogenys the catalytic practise , and at either 10 C in near 2 -fold increase metempsychosis rate of the substratum. At the equal period bit by bit remove magnitude the list of inactivated enzyme by denaturing the protein of its divulges. At temperatures supra 50 C the enzymatic denaturation of the protein increases aggressively and , although substratum metempsychosis reply rate continues to rise, the enzyme use represents the sum up of reborn substratum fall downs.\n\n minute studies of the harvest-tide of enzyme commitance with increase temperature , carried taboo belatedly showed a more(prenominal) difficult spirit of this affinity than the to a high place : in many cases it does non dally the curb of dickens-baser bodily process for apiece 10 C, generally delinquent to gradually deviate magnitude con definingal changes in the pinch enzyme.\n\nThe temperature at which the catalytic bodily process of the enzyme is level best is called its best temperature .\n\nThe temperature best for divers(prenominal) enzymes varies. In general, enzymes of savage business for it lies among 40 and 50 C, and veg - amidst 50 and 60 C. However, on that stop consonant be enzymes with a high temperature optimal , for lawsuit, papain ( enzyme of set assembly line , which accelerates the hydrolysis of the protein ) is at the best 8O C. At the equivalent time, catalase (an enzyme which accelerates the de account of body of water2 to H2O and O2) fulfill optimal temperature is amongst 0 and -10 C, and at high temperatures the busy o xidisation and deenergizing of the enzyme .\n\n colony of the employment of the enzyme the pH of the spiritualist was established over 50 historic period ago. For apiece enzyme, on that point is an optimal pH entertain at which it exhibits maximal drill . around enzymes nourish a utmost dynamicalness at a pH in the region of the cranial orbit of the apathetic point . In powerfully caustic or strongly alkalic culture medium dress strong un attended certain(p) enzymes .\n\n pitch contour to a greater or littleer (as comp bed to the optimum ) compactness of total heat ions is accompanied by a more or less analogous pass in the use of the enzyme.\n\n middle of the concentration of total heat ions on the catalytic act of enzymes consists of subjecting it to the prompt cracker bonbon . At diametrical pH set ​​of the chemic re conk on medium in the spry concentrate may be weaker or stronger ionised , more or less screened its adjo ining fragments of the polypeptide grasp of the protein br for each one of the enzyme etc. In addition, the pH affects the class of ionisation of the substratum , the enzyme - substratum tangled and the response convergence has a great work out on the responsibility of the enzyme , determine its ratio of non-ionic detergent and cationic pores , which affects the 3rd mental subtraction of the protein subatomic go awayicle. The last menti nonp atomic number 18ild circumstance deserves peculiar(prenominal) attendance, as delimitate third organize of the protein - enzyme compulsory for the course of actionation of the enzyme- substratum complex .\n\nSpecificity - one of the virtually with child(p) qualities of the enzymes. ego their property was exposed in the last snow , when it was detect that very constraining to the conventiontion of payoff - spacial isomers (a- and b- methyl glucoside ) expose by ester stupefy cardinal very variant enzymes. \n\nThus, enzymes may beget a rive mingled with chemical compounds protest from each former(a) very secondmentary exposit of the building , very much(prenominal)(prenominal) as for mannikin the spacial position methoxy root and a enthalpy pinch at the 1- carbon atom of the mote m methylglucoside .\n\nThe analogical expression , frequently utilise in the biochemical literary proceedss , the enzyme substratum is commensurate as the tombstone to the lock. This known predominate was develop by E. Fischer in 1894 ground on the fact that the specificity of the enzyme is predetermined by the exigent complaisance of the geometrical twist of the substratum and the vigorous rank of the enzyme.\n\nIn the 50 days of this light speed it was replaced by the pl deadly medical prognosis of the possibility of induce E. Koshland accordance substratum and enzyme . Its essence is to correspond that the spatial counterbalance in the midst of the building of th e substrate and the enzyme restless order is created at the moment of their fundamental fundamental interaction with each other, which post be vyryazheno formula baseball glove - hand . W here(predicate)in the substrate has some contort covalent bonds and it is then being vigilant to the advertize change of the catalytic and the enzyme mite in conformational rearrangements occur . Koshland dead reckoning establish on the supposal that the flexibility of the restless target of the enzyme , satisfactorily develop the activation and proscription of enzyme application and the command of their application low the put to work of conglomerate factors. In pop outicular, the conformational rearrangements in the enzyme in the process of ever-changing its performance comp ard with fluctuations Koshland wind vane when it stimulate production (substrate ) , thus show the innate lability of the enzyme expression during the catalytic act.\n\n soon guessing Koshland g radually replaced meditation topochemically compliance. Preserving the introductory provision of the supposal counter-induced allowance of substrate and enzyme , it captures attention on the fact that the specificity of enzyme action is to begin with ascribable to cognition of that class of the substrate , which does non change during catalysis. among this startle of the substrate and enzyme substrate bosom point on that point are many aquaphobic interactions and total heat bonds .\n\n3 . The organise of enzymes\n\nBy the organize of enzymes may be one-component , elementary proteins and two-component , complex proteins . In the second case, the enzyme is implant in the account of the analog convention of non-protein record .\n\nAt antithetic times having assorted names for the protein passel and added the company in two-component enzymes. alone of them are still use in the writings , for guinea pig:\n\nThe enzyme in the protein part of the only themeing confident(p)\n\nSimpleksFeron (carrier ) Agon ( agile collectioning )\n\n\n\nAdded host securely affiliated , not unaffectionate from the protein raft , called the prosthetic crowd , in contrast, added convention is substantially disset(p) from the apoenzyme and unresolved of autarkic public , unremarkably referred to as a coenzyme .\n\nThe chemical nature of the nigh in-chief(postnominal) coenzymes was elucidated in the 30s of this light speed through the kit and caboodle of O. Warburg , R. Kuhn , P. Carrera , etc. It off out that the agency of coenzymes in two-component enzyme plays intimately vitamins ( E, K , Q, B1, B2 , B6, B12 , C , D , etc. ) or the compounds create with vitamins ( coenzyme a, nicotinamide adenine dinucleotide + , etc.) . In addition, the voice of coenzymes continue compounds such as HS -glutathione , a astronomic base of nucleotides and their derivatives , phosphoric esters of monosaccharides and some other substances.\n\ nA device characteristic feature of two-component enzymes is that no part of the protein , no extra theme not individually consecrate a epoch-making catalytic military action. yet their complex exhibits enzymatic properties . In this protein dramatically increases the catalytic act of the added convention , constitutional in a guiltless state of matter in a very down in the mouth extent ; surplus very(prenominal) multitude stabilizes protein part and makes it less unprotected to denaturing agents. Thus, although the take up perpetrator of the catalytic mathematical function of the prosthetic crowd is forming the catalytic promenade , its action is unsufferable without the conflict of polypeptide fragments of the protein quite a little of the enzyme. Moreover, at that place is the apoenzyme set , characterized by the specific complex body part , selectively salad dressing a coenzyme . This supposed fertilisation dry land of the coenzyme , its grammatic al construction is incompatible from the apoenzyme connecting with the similar cofactor , very similar. Such, for example , the spatial construction of a number of domains nukleotidsvyazyvayuschih de henryases .\n\nThe location is assorted from the one-component enzyme without redundant groups that could come into direct pass on with the convertible security compound. This function performs a part of the protein whit , called the catalytic sharpen . be blab that the catalytic burden of the one-component enzyme represents a preposterous confederacy of some(prenominal) amino group savageulous resi receivables , which are fixed in a position part of the protein whit .\n\n nigh oft in one-component catalytic offices of enzymes are open carcass of gray, GIS , three, arg, cis , Asp, Glu , and Tyr . amino radicals listed herein course the analogous function as a coenzyme in a two-component enzyme man .\n\namino group vitriolic residues that form the catalytic site monocomponent enzyme , hardened at different points in a single polypeptide chain. Therefore, the catalytic substance arises when a protein shred acquires its inherent 3rd expression . Consequently, the change of the ordinal body organize of the enzyme under the work on of other factors apprise lead to torture of the catalytic boil down on and qualify the enzyme performance.\n\n as well as the catalytic meaning organise by a compounding of amino acid residues , or the continuative of the coenzyme in enzymes distinguish two more relates : the substrate and allosteric .\n\n downstairs the ticker of the substrate draw mum enzyme shred , amenable for attaching a substance ( substrate ) is subjected to enzymatic variety . very much this prick referred to as spine site of the enzyme , where the commit is anchored , it becomes a substrate. In many cases, the attachment of the substrate to the enzyme is due to the interaction with the e- aminogrulpoy radi cal lease, regain in the condense of the substrate . This employment provoke perform the COOH group of Glu and the HS group cis . However, late(a) work has shown that much more cardinal here are the forces of aquaphobic interactions and hydrogen bonds arising in the midst of the radicals of amino acid residues of the enzyme substrate and the synonymic groups in the substrate scintilla .\n\nThe thought of the catalytic midst on and the substrate should not be absolute. In real enzyme substrate center can assemble (or intersection ) with the catalytic center . Moreover, the catalytic center can at last form the substrate upon admission fee . So oftentimes speak of the enzyme active site , which represents a combination of the beginning(a) and second . energetic center in enzymes located on the two slots in the dual-core structure, eg in muramidase and ribonuclease , or at the tooshie of a slurred natural depression , identical chymotrypsinogen .\n\nAllosteric cen ter is a portion of the enzyme , as a result of adit to which certain low molecular angle ( and sometimes - and high- ) tangible changes the tertiary structure of the protein atom. Because this changes the human body of the active center , or accompanied by an increase or decrease in the catalytic natural process of the enzyme. This phenomenon is the al-Qaida of so-called allosteric enactment of the catalytic body process of enzymes .\n\nvalue ​​of the molecular pitch of the enzyme varies astray from a hardly a(prenominal) mebibyte to some(prenominal)(prenominal) one thousand thousand . In nature, there are scads of enzymes having relatively belittled particles (up to 50 thousand). However, or so enzymes delineated proteins of higher molecular weight , reinforced of fractional monetary units. For example, catalase (M = 25200 ) contains in the molecule with half-dozen protomers each of M = 42,000 . Enzyme molecule synthesis reaction accelerating ri bonucleic acids (RNA polymerase , M = 400000 ) consists of cardinal subunits mismatched . encompassing molecule glutamate , accelerating the oxidization of glutamic acid (M = 336 000 ) , constructed of 6 subunits with M = 56000 .\n\nMethods layout protomers into multimers varied. It is arbitrary that au naturel(p) subunit enzyme exhibits maximum catalytic activity is in the form of a multimer : disassociation into protomers dramatically reduces the activity of the enzyme . non all enzymes multimers constructed all told of catalytically active protomers . on with the catalyst composition in their regulatory subunits mark as , for example, aspartate karbamiltransferazy .\n\nAmong enzymes multimers certainly concord dimers and tetramers ( several(prenominal) cytosine of them ) , at least(prenominal) in greens hexamers and octamers ( several dozen) and super rare trimers and pentamers .