A Heat-stable Polypeptide Component of an ATP-dependent Proteolytic System from Reticulocytes.

The phosphoryl group is transferred to the Enzyme E I ( EI ), Histidine Protein ( HPr, Heat-stable Protein ) and Enzyme E II ( EII ) to a conserved histidine residue, whereas in the Enzyme E II B ( EIIB ) the phosphoryl group is usually transferred to a cysteine residue and rarely to a histidine.

Those found in the apoplast include hydrolytic enzymes such as proteases, lipases and glycosylases that act to degrade plant tissue, enzyme inhibitors to protect against host defence enzymes and necrotizing toxins.

Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the approximately 50 degradative enzymes of the lysosome that break apart biological matter.

* Some raw foodists believe that digestive enzymes in raw foods ( such as amylases, proteases, and lipases ) aid digestion.

Virulence factors include: pectinases, cellulases, ( which degrade plant cell walls ), and also proteases, lipases, xylanases and nucleases ( along with the normal virulence factors for pathogens – Fe acquisition, LPS integrity, multiple global regulatory systems ).

In this phase, complex molecules ( carbohydrates, lipids, and proteins ) are depolymerized into soluble compounds by hydrolytic enzymes ( cellulases, hemicellulases, amylases, lipases and proteases ).

Fats or lipids are broken down in the body by enzymes called lipases produced in the pancreas.

In the intestine, triglycerides are split into monoacylglycerol and free fatty acids in a process called lipolysis, with the secretion of lipases and bile, which are subsequently moved to absorptive enterocytes, cells lining the intestines.

Vegetable oils and animal fats contain mostly triglycerides, but are broken down by natural enzymes ( lipases ) into mono and diglycerides and free fatty acids.

The best characterized are the RTX toxins and the lipases.

The neutral lipids stored in adipocytes ( and in steroid synthesizing cells of the adrenal cortex, ovary, and testes ) in the form of lipid droplets, with a core of sterol esters and triacylglycerols surrounded by a monolayer of phospholipids, are coated with perilipin, a protein that acts as a protective coating from the body ’ s natural lipases, such as hormone-sensitive lipase ,.

In the uterus, the fetus is dependent on a high-carbohydrate diet, and lingual as well as gastric lipases are present in the fetus from 26 weeks of gestation on.

Beyerinck's auxanographic method was applied on several occasions by Eijkman, as for example during the secretion of enzymes which break down casein or bring about haemolysis, whereby he could demonstrate the hydrolysis of fats under the influence of lipases.

Triglycerides present on the VLDL undergo lipolysis by the cellular lipases of target tissues, which yields glycerol and free fatty acids.

Body odor is influenced by the actions of the skin flora, including members of Corynebacterium, which manufacture enzymes called lipases that break down the lipids in sweat to create smaller molecules like butyric acid.

* Lipolysis is carried out by lipases.

Besides leading to dry eyes, the obstructions can be degraded by bacterial lipases, resulting in the formation of free fatty acids, which irritate the eyes and sometimes cause punctate keratopathy.

Zymography can also be applied to other types of enzymes, including xylanases, lipases and chitinases.

* Fatty necrosis results from the action of lipases on fatty tissues ( e. g., acute pancreatitis, breast tissue necrosis ).

Special enzymes on the walls of blood vessels called lipoprotein lipases must break down triglycerides into free fatty acids and glycerol.

The reaction can also be accomplished with the help of enzymes ( biocatalysts ) particularly lipases ( E. C. 3. 1. 1. 3 ).

Microbial rancidity refers to a process in which microorganisms, such as bacteria, use their enzymes such as lipases to break down fat.

This results in increased production of cAMP, which activates protein kinase A, which subsequently activates lipases found in adipose tissue.

Other indicators include raised indicators of ampulla of vater ( pancreatic duct obstruction ) such as lipases and amylases.

Researchers have found that very good yields could be obtained from crude and used oils using lipases.

The use of lipases makes the reaction less sensitive to high FFA content which is a problem with the standard biodiesel process.

* lipases split fat into three fatty acids and a glycerol molecule.

Norepinephrine will react with lipases in brown fat to break down fat into triglycerides.

Caspases are proteins that are highly conserved, cysteine-dependent aspartate-specific proteases.

Agricultural Research Service scientists are interested in specialized enzymes called serine-class proteases that digest beta-amylases, which convert carbohydrates into " simple sugars " during the sprouting process.

Ingested proteins are then broken down into amino acids through digestion, which typically involves denaturation of the protein through exposure to acid and hydrolysis by enzymes called proteases.

Caspases are a important group of proteases involved in apoptosis.

Enzymes that carry out such reactions are called proteases.

After blood meal ingestion, proteases are active only in the posterior midgut.

Although it is not proven how elevated TGFβ levels are responsible for the specific pathology seen with the disease, an inflammatory reaction releasing proteases that slowly degrade the elastin fibers and other components of the extracellular matrix is known to occur.

For example within the serine proteases families are labelled Sx where S denotes the serine catalytic type and the x denotes the number of the family, for example S1 ( chymotrypsins ).

Alternatively, proteases may be classified by the optimal pH in which they are active:

Bacterial and fungal proteases are particularly important to the global carbon and nitrogen cycles in the recycling of proteins, and such activity tends to be regulated in by nutritional signals in these organisms.

Other proteases are present in leukocytes ( elastase, cathepsin G ) and play several different roles in metabolic control.

In nutrition, proteins are broken down through digestion by proteases back into free amino acids.

Active site cysteine residues are the functional unit in cysteine proteases.

PNAs are not easily recognized by either nucleases or proteases, making them resistant to enzyme degradation.

However, the proteases that recognize these cleavage sites are tissue-specific.

NK cells are cytotoxic ; small granules in their cytoplasm contain proteins such as perforin and proteases known as granzymes.

The coagulation factors are generally serine proteases ( enzymes ).

However specific proteases are used for cleaving of proteins for regulatory and protein trafficking purposes.

Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver.

It is thought that the bactericidal properties of HClO are enough to kill bacteria phagocytosed by the neutrophil, but this may instead be a step necessary for the activation of proteases.

The mite's gut contains potent digestive enzymes ( notably proteases ) that persist in their feces and are major inducers of allergic reactions such as wheezing.

Caspases, or cysteine-aspartic proteases or cysteine-dependent aspartate-directed proteases are a family of cysteine proteases that play essential roles in apoptosis ( programmed cell death ), necrosis, and inflammation.