Enzymes are biologic polymers that catalyze the chemical reactions that make life as we know it possible.

The
presence and maintenance of a complete and balanced set of enzymes is essential for the breakdown of
nutrients to supply energy and chemical building blocks; the assembly of those building blocks into proteins,
DNA, membranes, cells, and tissues; and the harnessing of energy to power cell motility, neural function, and
muscle contraction. With the exception of catalytic RNA molecules, or ribozymes, enzymes are proteins. The
ability to assay the activity of specific enzymes in blood, other tissue fluids, or cell extracts aids in the diagnosis
and prognosis of disease. Deficiencies in the quantity or catalytic activity of key enzymes can result from
genetic defects, nutritional deficits, or toxins. Defective enzymes can result from genetic mutations or
infection by viral or bacterial pathogens (eg, Vibrio cholerae). Medical scientists address imbalances in enzyme
activity by using pharmacologic agents to inhibit specific enzymes and are investigating gene therapy as a
means to remedy deficits in enzyme level or function. In addition to serving as the catalysts for all metabolic
processes, their impressive catalytic activity, substrate specificity, and stereospecificity enable enzymes to
fulfill key roles in other processes related to human health and well-being. The absolute stereospecificity
of enzymes is of particular value for use as soluble or immobilized catalysts for specific reactions in the
synthesis of a drug or antibiotic. Proteolytic enzymes augment the capacity of detergents to remove dirt and
stains. Enzymes play an important role in producing or enhancing the nutrient value of food products for both
humans and animals. The protease rennin, for example, is utilized in the production of cheeses while lactase is
employed to remove lactose from milk for the benefit of persons who suffer from lactose intolerance as a
consequence of a deficiency in this hydrolytic enzyme (Chapter 43).

Enzim adalah polimer biologis yang mengkatalisasi reaksi kimia yang membuat kehidupan
seperti yang kita kenal mungkin. Kehadiran dan pemeliharaan seperangkat enzim yang
lengkap dan seimbang sangat penting untuk pemecahan nutrisi untuk memasok energi dan
bahan kimia pembangun; perakitan blok-blok pembangun menjadi protein, DNA, membran,
sel, dan jaringan; dan pemanfaatan energi untuk menggerakkan motilitas sel, fungsi saraf,
dan kontraksi otot. Dengan pengecualian molekul RNA katalitik, atau ribozim, enzim adalah
protein. Kemampuan untuk menguji aktivitas enzim spesifik dalam darah, cairan jaringan
lain, atau ekstrak sel membantu dalam diagnosis dan prognosis penyakit. Kekurangan dalam
jumlah atau aktivitas katalitik dari enzim-enzim utama dapat disebabkan oleh cacat genetik,
kekurangan nutrisi, atau racun. Enzim yang rusak dapat dihasilkan dari mutasi genetik atau
infeksi oleh virus atau bakteri patogen (misalnya, Vibrio cholerae). Ilmuwan medis
mengatasi ketidakseimbangan dalam enzim
aktivitas dengan menggunakan agen farmakologis untuk menghambat enzim spesifik dan
sedang menyelidiki terapi gen sebagai sarana untuk memperbaiki defisit di tingkat atau
fungsi enzim. Selain berfungsi sebagai katalis untuk semua proses metabolisme, aktivitas
katalitiknya yang mengesankan, spesifisitas substrat, dan stereospecificity memungkinkan
enzim untuk memenuhi peran kunci dalam proses lain yang berkaitan dengan kesehatan
dan kesejahteraan manusia. Stereositif mutlak
enzim adalah nilai tertentu untuk digunakan sebagai katalis terlarut atau tidak bergerak
untuk reaksi spesifik dalam sintesis obat atau antibiotik. Enzim proteolitik menambah
kapasitas deterjen untuk menghilangkan kotoran dan noda. Enzim memainkan peran
penting dalam memproduksi atau meningkatkan nilai nutrisi produk makanan untuk
manusia dan hewan. Protease rennin, misalnya, digunakan dalam produksi keju sementara
laktase digunakan untuk menghilangkan laktosa dari susu untuk kepentingan orang yang
menderita intoleransi laktosa sebagai konsekuensi dari kekurangan enzim hidrolitik ini (Bab
43).

ENZYMES ARE EFFECTIVE & HIGHLY SPECIFIC CATALYSTS

The enzymes that catalyze the conversion of one or more compounds (substrates) into one or more different
compounds (products) enhance the rates of the corresponding noncatalyzed reaction by factors of at least 106.
Like all catalysts, enzymes are neither consumed nor permanently altered as a consequence of their
participation in a reaction. In addition to being highly efficient, enzymes are also extremely selective catalysts.
Unlike most catalysts used in synthetic chemistry, enzymes are specific both for the type
of reaction catalyzed and for a single substrate or a small set of closely related substrates. Enzymes are also
stereospecific catalysts and typically catalyze reactions of only one stereoisomer
of a given compound—for example, D- but not L-sugars, L- but not D-amino acids. Since they bind substrates
through at least “three points of attachment,” enzymes can even convert nonchiral substrates to chiral
products. Figure 7–1 illustrates why the enzyme-catalyzed reduction of the nonchiral substrate pyruvate
produces L-lactate—rather than a racemic mixture of D- and L-lactate. The exquisite specificity of enzyme
catalysts imbues living cells with the ability to simultaneously conduct and independently control a broad
spectrum of chemical processes.

ENZYMES ARE CLASSIFIED BY REACTION TYPE

The commonly used names for most enzymes describe the type of reaction catalyzed, followed by the suffix -
ase. For example, dehydrogenases remove hydrogen atoms, proteases hydrolyze proteins, and isomerases
catalyze rearrangements in configuration. Modifiers may precede the name to indicate
the substrate (xanthine oxidase), the source of the enzyme (pancreatic ribonuclease), its regulation (hormone-
sensitive lipase), or a feature of its mechanism of action (cysteine protease).
Where needed, alphanumeric designators are added to identify multiple forms of an enzyme (eg, RNA
polymerase III; protein kinase Cβ). To address ambiguities, the International Union of Biochemists
(IUB) developed an unambiguous system of enzyme nomenclature in which each enzyme has a unique name
and code number that identify the type of reaction catalyzed and the substrates involved. Enzymes are
grouped into six classes:
1. Oxidoreductases (catalyze oxidations and reductions)
2. Transferases (catalyze transfer of moieties such as glycosyl, methyl, or phosphoryl groups)
3. Hydrolases (catalyze hydrolytic cleavage of C—C, C—O, C—N, and other bonds)
4. Lyases (catalyze cleavage of C—C, C—O, C—N, and other bonds by atom elimination, leaving double bonds)
5. Isomerases (catalyze geometric or structural changes within a molecule)
6. Ligases (catalyze the joining together of two molecules coupled to the hydrolysis of ATP) Despite the clarity of
the IUB system, the names are lengthy and relatively cumbersome, so we generally continue to refer
to enzymes by their traditional, albeit sometimes ambiguous names. The IUB name for hexokinase illustrates
both the clarity of the IUB system and its complexities. The IUB name of hexokinase is ATP:D-hexose 6-
phosphotransferase E.C.
2.7.1.1. This name identifies hexokinase as a member of class 2 (transferases), subclass 7 (transfer of a
phosphoryl group), subsubclass 1 (alcohol is the phosphoryl acceptor), and “hexose-6” indicates that the
alcohol phosphorylated is on carbon six of a hexose. However, we continue to call it hexokinase.