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847 12359 Ensembl ENSG00000121691 ENSMUSG00000027187 UniProt P04040 P24270 RefSeq (mRNA) NM_001752 NM_009804 RefSeq (protein) NP_001743 NP_033934 Location (UCSC) Chr 11: 34.44 – 34.47 Mb Chr 2: 103.28 – 103.32 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals ...
These three enzymes are particularly effective in breaking down the cell walls of yeast, so C. cellulans is considered a major source of yeast-lytic enzymes. [ 12 ] C. cellulans produce a variety of degradative enzymes, such as beta-glucosidase, protease, glycoside hydrolase, and chitinase.
Lactoperoxidase (LPO, EC 1.11.1.7) is a peroxidase enzyme secreted from mammary, salivary, tears and other mucosal glands including the lungs, bronchii and nose [5] that function as a natural, first line of defense against bacteria and viral agents. [6] Lactoperoxidase is a member of the heme peroxidase family of enzymes.
The enzyme catalase, found primarily in peroxisomes and the cytosol of erythrocytes (and sometimes in mitochondria [12]), converts the hydrogen peroxide into water and oxygen. Peroxisomal β-oxidation also requires enzymes specific to the peroxisome and to very long fatty acids.
Catalases are enzymes that catalyse the conversion of hydrogen peroxide to water and oxygen, using either an iron or manganese cofactor. [104] [105] This protein is localized to peroxisomes in most eukaryotic cells. [106] Catalase is an unusual enzyme since, although hydrogen peroxide is its only substrate, it follows a ping-pong mechanism.
However the last enzyme is absent in humans, explaining the disease known as gout, caused by the accumulation of uric acid. Certain enzymes within the peroxisome, by using molecular oxygen, remove hydrogen atoms from specific organic substrates (labeled as R), in an oxidative reaction, producing hydrogen peroxide (H 2 O 2, itself toxic):
Monoamine oxidases (MAO) (EC 1.4.3.4) are a family of enzymes that catalyze the oxidation of monoamines, employing oxygen to clip off their amine group. [1] [2] They are found bound to the outer membrane of mitochondria in most cell types of the body. The first such enzyme was discovered in 1928 by Mary Bernheim in the liver and was named ...
The enzymes catalyze a reductive elimination of iodine (the different isoforms attack different thyronine positions), thereby oxidizing themselves similar to Prx, followed by a reductive recycling of the enzyme. Iodotyrosine deiodinase contributes to breakdown of thyroid hormones.