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Carbohydrase is the name of a set of enzymes that catalyze five types of reactions, turning carbohydrates into simple sugars, from the large family of glycosidases. [1] Carbohydrases are produced in the pancreas, salivary glands and small intestine, breaking down polysaccharides.
GCSE Bitesize was launched in January 1998, covering seven subjects. For each subject, a one- or two-hour long TV programme would be broadcast overnight in the BBC Learning Zone block, and supporting material was available in books and on the BBC website. At the time, only around 9% of UK households had access to the internet at home.
Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.
5′-Nucleotidase (EC 3.1.3.5) is an enzyme which catalyzes the phosphorylytic cleavage of 5′-nucleotides. [2] Although originally found in snake venom, [ 3 ] the activity of 5'nucleotidase has been described for bacteria and plant cells, and is widely distributed in vertebrate tissue. [ 4 ]
Typical eukaryotic cell. Cellular respiration is the process by which biological fuels are broken down in the presence of a hydrogen acceptor, such as oxygen, to drive the production of adenosine triphosphate (ATP), which stores chemical energy in a biologically accessible form.
Enzymes can be classified by two main criteria: either amino acid sequence similarity (and thus evolutionary relationship) or enzymatic activity. Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase.
Similarly, another crucial site for the functionality of an enzyme is the active-site, which should also be maintained while enzyme is being attached to a surface for immobilization, it is a must to have a selective method for the attachment of surface/material to not end up with an immobilized, but dysfunctional enzyme. [3]
The enzyme DNA-(apurinic or apyrimidinic site) lyase, also referred to as DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase (systematic name) or DNA AP lyase (EC 4.2.99.18) catalyzes the cleavage of the C-O-P bond 3' from the apurinic or apyrimidinic site in DNA via β-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. [1]