Specifically, urease catalyzes the hydrolysis of urea to produce ammonia and carbamate, the carbamate produced is subsequently degraded by means of spontaneous hydrolysis to produce another molecule of ammonia and carbonic acid. [1] Urease activity tends to increase the pH of the medium in which it is due to the production of ammonia. It is produced by bacteria, fungi and several higher plants. Urease, functionally, belongs to the superfamily of amidohydrolases and phosphotriesterases. [2]
The structural variations that can happen in a protein after translation to make it function appropriately are:
• Folding – In the cytoplasm it partakes chaperonin protein that will aid to fold the protein into a purposeful shape. The hydrogen bonds will form to create secondary protein and disulfide bonds will form tertiary structure and hydrogen bonds.
• Cleavage – The activation into a purposeful protein over cleavage of certain amino acid sequences in which the amino acid order can fold to form the secondary or tertiary structure.
• Chemical Modification – A method of chemically responding a protein or nucleic acid with chemical components.
• Elaboration – In particulars of folding, chaperones, kinds of bonds, the role of Golgi, combination into current molecular arrays. Etc.
B and f i think since more population means more resource consumption
If you're referring to the book, the author is Nicholas Moreno.
