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A protein that has enzymatic (ase) activity.That is,it can cleave other proteins (prot) at specific amino acid sequences.
Contrast a nuclease, which is a protein that has enzymatic (ase) activity. It is able to cleave nucleic (nuc) acids.
All about the prefixes and the suffixes.
What else can I help you with?
In what locations can proteasome be located?
Proteasomes are protein complexes. These protein complexes are present in eukaryotes, some bacteria and in archaea. The proteasomes are located in the nucleus and the cytoplasm when looking at eukaryotes.
What is responsible for identifying and digesting damaged or denatured proteins?
Proteasomes are responsible for identifying and digesting damaged or denatured proteins. Proteasomes are large protein complexes that are found in eukaryotic cells.
Who discovered proteasomes?
Proteasomes were discovered by researchers who were studying protein degradation within cells. The key discovery came in the 1980s by a group led by Aaron Ciechanover, Avram Hershko, and Irwin Rose, who identified the ubiquitin-mediated proteolysis pathway and elucidated the role of proteasomes in protein breakdown. Their work laid the foundation for understanding how cells regulate protein levels and maintain cellular function. In 2004, the trio was awarded the Nobel Prize in Chemistry for their contributions to this field.
Where does protein degradation occur in the body?
Protein degradation occurs in the body primarily in the proteasomes, which are specialized structures within cells responsible for breaking down and recycling proteins that are no longer needed.
What is it called when an enzymes active site loses its shape?
When this happens to a protein, it is said to denature.Denature is caused commonly by very high or low temperature,concentrated acids or bases.Denature by high temperature is irrevesible.
Enzyme complexes that break down protein are called?
Proteases are enzymes that degrade/digest proteins
Waste products in the cell accumulate and are eventually?
broken down by cellular machinery such as lysosomes and proteasomes, or transported out of the cell for excretion. This process helps maintain cellular health and prevents harmful buildup of waste products that can interfere with normal cellular function.
How are enzymes degraded?
Enzymes are degraded by proteolytic enzymes that break down the peptide bonds in the protein structure. This degradation can occur in lysosomes, which contain acidic hydrolases, or in the cytoplasm with the help of proteasomes. Enzyme degradation is important for regulating enzyme levels and activity in the cell.
What organelle is responsible for identifying and digesting damaged or denatured proteins?
The proteasome is responsible for identifying and degrading damaged or denatured proteins within the cell. It recognizes specific signals on the proteins that mark them for degradation, and then breaks them down into smaller peptides.
What is need to degraded a bio molecule?
Degradation of a biomolecule typically requires specific enzymes that catalyze the breakdown of the molecule into smaller units, such as monomers. This process often involves hydrolysis or oxidation reactions, which can be facilitated by environmental factors such as pH, temperature, and the presence of co-factors or other molecules. Additionally, cellular machinery, such as lysosomes or proteasomes, may be involved in the controlled degradation of biomolecules within living organisms.
What would happen initially to cells that lack a functional ubiquitin?
Cells that lack a functional ubiquitin system would have impaired protein degradation through the proteasome pathway. This can lead to accumulation of misfolded or damaged proteins, leading to cellular stress and dysfunction. Ultimately, it may result in cell death or contribute to the development of various diseases.
Function of protease?
Proteases are protein-digesting enzymes. They are produced in the stomach, pancreas, salivary glands, and small intestine. They break long-chain proteins (polypeptides) into shorter polypeptides and individual amino acids, of which there are around twenty.
