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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
The type III copper can be replaced by Hg(II), which causes a decrease in laccase activity. [1] Cyanide removes all copper from the enzyme, and re-embedding with type I and type II copper has been shown to be impossible. Type III copper, however, can be re-embedded back into the enzyme. A variety of other anions inhibit laccase. [9]
If an enzyme needs coenzyme to work itself, it is called an apoenzyme. In fact, it alone cannot catalyze reactions properly. Only when its cofactor comes in and binds to the active site to form holoenzyme does it work properly. One example of the coenzyme is Flavin. It contains a distinct conjugated isoalloxazine ring system.
The two enzymes have similar folding patterns and protein domains. In fact, past attempts to produce drugs targeting glucansucrase have not been successful because the drugs also disrupted amylase, which is necessary to break down starches. [12] [13] This occurred because the active sites of the two enzymes are nearly the same. Glucansucrase ...
Adenosine triphosphate Adenosine diphosphate Adenosine monophosphate. ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca 2+ + Mg 2+)-ATPase, HCO 3 −-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP ...
DNase enzymes can be inhaled using a nebulizer by cystic fibrosis sufferers. DNase enzymes help because white blood cells accumulate in the mucus, and, when they break down, they release DNA, which adds to the 'stickiness' of the mucus. DNase enzymes break down the DNA, and the mucus is much easier to clear from the lungs.
PLP is covalently attached to the enzyme via a Schiff Base linkage formed by the condensation of its aldehyde group with the ε-amino group of an enzymatic Lys residue. The Schiff base, which is conjugated to the enzyme's pyridinium ring, is the focus of the coenzyme activity. Ping Pong Bi Bi mechanism of PLP dependent enzyme catalyzed ...
Endo-1,4-β-xylanase (EC 3.2.1.8, systematic name 4-β-D-xylan xylanohydrolase) is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, [1] thus breaking down hemicellulose, one of the major components of plant cell walls: Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans