An enzyme is a kind of macromolecule substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process and most enzymes are proteins. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes.
In the catalytic enzyme reaction system, reactant molecules are called substrate. The substrate can be transformed to another molecule. Without enzymes, many of these reactions would not take place at an apparent rate. Enzymes can catalyze all aspects of cell metabolism, involving the digestion of food (large nutrient molecules are broken down into smaller molecules), the conservation and transformation of chemical energy, and the construction of cellular macromolecules from smaller precursors.
Like all catalysts, enzymes accelerate the reaction rate via lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds.
Enzyme activity is affected by various factors, including substrate concentration and the presence of inhibiting molecules. Generally speaking, the rate of an enzymatic reaction increases with increased substrate concentration, reaching maximum velocity when all active sites of the enzyme molecules are engaged. Additionally, besides the two factors above, there is another factor affecting enzyme activity named allosteric control. It involves stimulation of enzyme action as well as inhibition. Allosteric stimulation and inhibition allow production of energy and materials by the cell when they are needed and inhibit production when the supply is adequate.
CUSABIO provides several excellent enzyme products. All of them have been sold with high-quality and good biological activities. The purity of most active proteins are higher than 97%, and all of which have been validated activity and low endotoxin, stored in freeze-dried powder form for best stability, majority tag-free thus closer to native protein. Here, we numerate several pictures of hot enzymes.
Recombinant Streptococcus sp Streptokinase G protein (skg) (CSB-AP000171SNC)
Recombinant Staphylococcus phage 42D protein (sak) (CSB-AP000181BDN)
Here, we introduce the function of CUSABIO enzyme as follows:
Persephin, also abbreviated as PSPN, is a disulfide-linked, homodimeric, neurotrophic factor structurally related to glial cell line-derived neurotrophic factor (GDNF), artemin, and neurturin. PSPN signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for PSPN. PSPN promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching.
Superoxide dismutase [Cu-Zn] (SOD1), one of three human superoxide dismutases, is a 32 kDa homodimer which forms a β-barrel and contains an intramolecular disulfide bond and a binuclear Cu/Zn site in each subunit, located on chromosome 21. SOD1 has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. It is implicated in apoptosis and familial amyotrophic lateral sclerosis.
The TP53-inducible glycolysis and apoptosis regulator, also known as fructose-2,6-bisphosphatase or TIGAR, acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Additionally, TIGAR also plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity.