Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is

an enzyme that in humans is encoded by the GSR gene. Glutathione reductase (EC 1.8.1.7)
catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH),
which is a critical molecule in resisting oxidative stress and maintaining the reducing environment
of the cell.[5][6][7] Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes
an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar
equivalents of GSH:

General reaction catalyzed by glutathione reductase

The glutathione reductase is conserved between all kingdoms. In bacteria, yeasts, and animals,
one glutathione reductase gene is found; however, in plant genomes, two GR genes are
encoded. Drosophila and trypanosomes do not have any GR at all.[8] In these organisms,
glutathione reduction is performed by either the thioredoxin or the trypanothione system,
respectively.[8][9]

Glutathione peroxidase (GPx) (EC 1.11.1.9) is the general name of an enzyme family
with peroxidase activity whose main biological role is to protect the organism from oxidative
damage. The biochemical function of glutathione peroxidase is to reduce lipidhydroperoxides to
their corresponding alcohols and to reduce free hydrogen peroxide to water.

Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes

the dismutation (or partitioning) of the superoxide(O2−) radical into either ordinary
molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of
oxygen metabolism and, if not regulated, causes many types of cell damage.[2] Hydrogen
peroxide is also damaging and is degraded by other enzymes such as catalase. Thus, SOD is an
important antioxidant defense in nearly all living cells exposed to oxygen. One exception
is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent
damage from reactive (O2−).

Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such
as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen
peroxide to water and oxygen.[5] It is a very important enzyme in protecting the cell from oxidative
damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover
numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide
molecules to water and oxygen each second.[6]
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[7] It contains
four iron-containing heme groups that allow the enzyme to react with the hydrogen peroxide. The
optimum pH for human catalase is approximately 7,[8] and has a fairly broad maximum: the rate of
reaction does not change appreciably between pH 6.8 and 7.5.[9] The pH optimum for other
catalases varies between 4 and 11 depending on the species.[10] The optimum temperature also
varies by species.[11]
Alpha tocopherol is the strongest of several forms of tocopherol elements that scientists and
nutritionists call "vitamin E" and are found naturally in a variety of foods. Some foods contain
alpha tocopherol and others contain gamma tocopherol, a less powerful tocopherol, though
scientists have found that the human body can transform the gamma tocopherol into a similar
end result.

Alpha tocopherol and other vitamin E substances are antioxidants, which means they can help
the body fight off a range of degenerative conditions. Vitamin E is beneficial to overall body
function, and a regular part of a healthy diet. As far as specific health effects of increased alpha
tocopherol consumption, some studies differ on how the essential element might affect heart
health. Tocopherol has been known to interact poorly with blood thinners. Other health risks may
also apply to elevated levels of alpha tocopherol in a daily diet. The RDA or recommended daily
allowance for an adult male is 15mg/day.

Salah satu senyawa dalam tubuh yang bersifat antioksidan adalah taurine. Taurine merupakan asam
amino semi esensial yang mengandung gugus belerang dalam struktur kimianya (Guz dkk., 2007).
Taurine memainkan beragam fungsi dalam tubuh, seperti menjaga stabilitas membran,
osmoregulator, neuromodulasi, detoksifikasi, pembentuk otak dan retina mata serta antioksidan
yang mencegah kerusakan oksidatif pada banyak jaringan tubuh. Sebagai antioksidan, taurine
berperan untuk menjaga stabilitas membran sel, mengikat ROS dan menurunkan peroksidasi lemak.
Selain itu, taurine juga mampu mengikat asam hipoklorit yang berasal dari hasil aktivasi granulosit
dan membentuk ikatan taurine-kloramin

Hypotaurine is a sulfinic acid that is an intermediate in the biosynthesis of taurine. Like taurine, it
also acts as an endogenousneurotransmitter via action on the glycine receptors.[1]
Hypotaurine is derived from cysteine (and homocysteine). In mammals, the biosynthesis of
hypotaurine from cysteine occurs in the pancreas. In the cysteine sulfinic
acid pathway, cysteine is first oxidized to its sulfinic acid, catalyzed by the enzyme cysteine
dioxygenase. Cysteine sulfinic acid, in turn, is decarboxylated by sulfinoalanine decarboxylase to
form hypotaurine. Hypotaurine is enzymatically oxidized to yield taurine by hypotaurine
dehydrogenase.[2]

Epinefrin (juga dikenal sebagai adrenalin) dilepaskan oleh kelenjar adrenalin dan bertanggung jawab
untuk pengaturan respon tubuh”melawan atau lari”. Ini mengatur transfer sinyal saraf antara
neuron dan sel-sel tubuh dan meningkatkan laju dan kekuatan kontraksi jantung. Epinefrin biasanya
dilepaskan ketika seseorang berada dalam tekanan atau kegembiraan.

Keadaan stres akan merangsang pengeluaran hormon epinefrin secara berlebihan sehingga menyebabkan
jantung berdebar keras dan cepat. Hormon epinefrin diproduksi dalam jumlah banyak pada saat sedang marah.
Indikasi stres adalah sulit tidur, cepat lelah, mudah terusik, kepala pusing, dan sebagainya. Penderita stres
umumnya juga kehilangan nafsu makan.

Asam laktat merupakan produk hasil metabolisme karbohidrat tanpa menggunakan oksigen
(metabolisme anaerob). Asam laktat diproduksi di sel otot saat suplai oksigen tidak mencukupi untuk
menunjang produksi energi. Produk asam laktat normal terdapat di dalam tubuh manusia.

Piruvat adalah suatu senyawa kimia yang penting dalam biokimia. Senyawa ini merupakan
hasil metabolisme glukosa yang disebut glikolisis. Sebuah molekul glukosa terpecah menjadi
dua molekul asam piruvat, yang kemudian digunakan untuk menghasilkan energi. Jika tersedia
cukup oksigen, maka asam piruvat diubah menjadi asetil-KoA, yang kemudian diproses
dalam siklus Krebs. Piruvat juga dapat diubah menjadi oksaloasetat melalui reaksi
anaploretik yang kemudian dipecah menjadi molekul-molekul karbon dioksida.