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Lactase (EC 3.2.1.108) is an enzyme produced by many organisms and is essential to the complete digestion of whole milk. It breaks down the sugar lactose into its component parts, galactose and glucose. Lactase is found in the brush border of the small intestine of humans and other mammals.
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen. [5] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS).
Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the monomer of 4-oxalocrotonate tautomerase, [27] to over 2,500 residues in the animal fatty acid synthase. [28] Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. [29]
Function: An enzyme that is produced by animals that forms part of the innate immune system and is abundant in the secretions of saliva, human milk, tears, and mucus. It functions as an antimicrobial agent by splitting the peptidoglycan component of bacterial cell walls, which then leads to cell death.
Ribbon representation of the Streptomyces lividans β-1,4-endoglucanase catalytic domain - an example from the family 12 glycoside hydrolases [1]. Cellulase (EC 3.2.1.4; systematic name 4-β-D-glucan 4-glucanohydrolase) is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.
In bacteria, secreted elastase breaks down host connective tissue proteins, causing tissue damage and inflammation. As a result, it's considered a virulence factor. [9] Elastases of the serine protease type preferentially break down peptide bonds on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine.
Bacterial enzymes are bacterial proteins whose main functions include catalytic operations. Pages in category "Bacterial enzymes" The following 28 pages are in this category, out of 28 total.