http___livro-ensino-medio.f1cf.com.br_fisica_hr_physics-111.html_1.xml
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An enzyme or protein catalyst (amylase, maltase and pepsin, etc.) becomes not only facilitates the passage of atoms from one place to another. That done, the enzyme is ready todo it with the next molecule, like a machine in a factory. Maxie is also this facilitator, he leaves with a certain type of molecule that can move from one place to another without it requires an extra dose of energy. There are approximately 3700 different types of enzymes are currently classified. Some of these enzymes are present in one cell type, as in the case of enzymes that convert tyrosina to dopamine, a neurotransmitter nerve cells. But there are enzymes that are present in most cells, such as that participates in the conversion of glucose and oxygen to carbon dioxide and water. The reactions of the enzymes involved and occur easily in nature are extremely difficult to be reproduced in the laboratory. These occur only under conditions of high temperature, pressure or low pH values. However, the enzymes operate effectively in an environment of temperature 37 ° C, 1 atm pressure and pH 7 (neutral pH), or a value or basic or acidic. Warming orvarying pH (hydrogen potential) of enzymes, some form of protein can lead to destruction of its tertiary structure (shape protein). With this, the enzymes lose their biological action. This phenomenon is called protein denaturation. Egby heating the egg white albumin is denatured (the process is irreversible). The proteins have the primary structure, secondary and tertiary. The primary structure of a protein is determined by the sequence of amino acids in its chain. Related to the spatial arrangement of the primary structures, which can be helical or pleated sheet is secondary structure. The spatial form of a protein, caused by the secondary winding of structures is called the tertiary structure of the protein. This winding is not random but targeted protein function. Some proteins such as hemoglobin, have structures formed by the association of two or more polypeptide chains, constituting the up-quaternary structure. (adapted from Junqueira and Lamb, 2005)
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Enzim ili proteina katalizator (amilaza, maltaza i pepsina, itd.) postaje ne samo da olakšava prolaz atoma s jednog mjesta na drugo. To učinili, enzim je spremanto učiniti sa sljedećom molekulom, kao stroj u tvornici. Maxie je to moderator, on ostavlja s određenim vrstama molekula koje se mogu premjestiti s jednog mjesta na drugo bez da zahtijeva dodatnu dozu energije. Postoji oko 3700 različitih vrsta enzima su trenutno klasificirani. Neki od tih enzima su prisutni u jednom tip stanica, kao u slučaju enzima koji pretvaraju tyrosina dopamina, neurotransmitera živčanih stanica. No, tu su enzimi koji su prisutni u većini stanica, kao što su to sudjeluje u pretvorbi glukoze i kisika na ugljikov dioksid i vodu. Reakcije enzima koji su uključeni i jednostavno se javljaju u prirodi su izuzetno teško se reproducirati u laboratoriju. Ovo se pojavljuje samo u uvjetima visoke temperature, tlaka ili niskim pH vrijednostima. Međutim, enzimi djeluju učinkovito u okruženju temperature 37 ° C, 1 atm tlak i pH 7 (neutralna pH), odnosno vrijednost ili osnovni ili kisela. Zagrijavanje ilipromjenom pH (potencijal vodika) enzima, neki oblik proteina može dovesti do uništenja njegove tercijarne strukture (oblik proteina). Uz to, enzimi gube biološku akciju. Ovaj fenomen se naziva denaturacije proteina. Ex:grijanje bjelanjak albumin denaturira (proces nepovratan). Proteini imaju primarnu strukturu, sekundarne i tercijarne. Primarne strukture proteina određena je slijed aminokiselina u svom lancu. Vezano za prostorno uređenje osnovnih struktura koje mogu biti spiralne ili nabrane list sekundarne strukture. Prostorni oblik proteina, uzrokovan sekundarnog namota struktura se zove tercijarna struktura proteina. Ovo navijanje nije slučajan, ali ciljano proteina funkciju. Neki proteina, kao što su hemoglobin, imaju strukturu formirane u organizaciji dvaju ili više polipeptidnih lanaca, konstituiranju up-kvaternog strukturu. (Preuzeto iz Junqueira i Lamb, 2005)