Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.
Neomycin is an aminoglycoside antibiotic that displays bactericidal activity against gram-negative aerobic bacilli and some anaerobic bacilli where resistance has not yet arisen. It is generally not effective against gram-positive bacilli and anaerobic gram-negative bacilli. Neomycin comes in oral and topical formulations, including creams, ointments, and eyedrops. Neomycin belongs to the aminoglycoside class of antibiotics that contain two or more amino sugars connected by glycosidic bonds.
L-Gulonolactone oxidase is an enzyme that produces vitamin C, but is non-functional in Haplorrhini, in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action.
Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopterin are: MPT and pyranopterin-dithiolate. The nomenclature for this biomolecule can be confusing: Molybdopterin itself contains no molybdenum; rather, this is the name of the ligand that will bind the active metal. After molybdopterin is eventually complexed with molybdenum, the complete ligand is usually called molybdenum cofactor.
(S)-Tetrahydroberberine oxidase is an enzyme that catalyzes the final transformation in the biosynthesis of berberine, a quaternary benzylisoquinoline alkaloid of the protoberberine structural subgroup. This reaction pathway catalyzes the four-electron oxidation of (S)-tetrahydroberberine in the presence of oxygen to produce berberine and hydrogen peroxide as products.
In enzymology, a reticuline oxidase (EC 1.21.3.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a cholesterol oxidase (EC 1.1.3.6) is an enzyme that catalyzes the chemical reaction
Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for energy or industrial use, as well as in other fungi, plants, and bacteria.
In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase (EC 1.17.99.3) is an enzyme that catalyzes the chemical reaction
Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
The enzyme dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) catalyzes the chemical reaction
Aminoglycoside-3'-phosphotransferase, also known as aminoglycoside kinase, is an enzyme that primarily catalyzes the addition of phosphate from ATP to the 3'-hydroxyl group of a 4,6-disubstituted aminoglycoside, such as kanamycin. However, APH(3') has also been found to phosphorylate at the 5'-hydroxyl group in 4,5-disubstituted aminoglycosides, which lack a 3'-hydroxyl group, and to diphosphorylate hydroxyl groups in aminoglycosides that have both 3'- and 5'-hydroxyl groups. Primarily positively charged at biological conditions, aminoglycosides bind to the negatively charged backbone of nucleic acids to disrupt protein synthesis, effectively inhibiting bacterial cell growth. APH(3') mediated phosphorylation of aminoglycosides effectively disrupts their mechanism of action, introducing a phosphate group that reduces their binding affinity due to steric hindrances and unfavorable electrostatic interactions. APH(3') is primarily found in certain species of gram-positive bacteria.
The aminocyclitols are compounds related to cyclitols. They possess features of relative and absolute configuration that are characteristic of their class and have been extensively studied; but these features are not clearly displayed by general methods of stereochemical nomenclature, so that special methods of specifying their configuration are justified and have long been used. In other than stereochemical respects, their nomenclature should follow the general rules of organic chemistry.
Paromamine 6'-oxidase (EC 1.1.3.43, btrQ (gene), neoG (gene), kanI (gene), tacB (gene)) is an enzyme with systematic name paromamine:oxygen 6'-oxidoreductase. This enzyme catalyses the following chemical reaction
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction
UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ribostamycin N-acetylglucosaminyltransferase. This enzyme catalyses the following chemical reaction
Neamine transaminase is an enzyme with systematic name neamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
Neomycin C transaminase is an enzyme with systematic name 2-oxoglutarate:neomycin C aminotransferase. This enzyme catalyses the following chemical reaction
2'-N-acetylparomamine deacetylase (EC 3.5.1.112, btrD (gene), neoL (gene), kanN (gene)) is an enzyme with systematic name 2'-N-acetylparomamine hydrolase (acetate-forming). This enzyme catalyses the following chemical reaction
2'''-acetyl-6'''-hydroxyneomycin C deacetylase (EC 3.5.1.113, neoL (gene)) is an enzyme with systematic name 2'''-acetyl-6'''-hydroxyneomycin C hydrolase (acetate-forming). This enzyme catalyses the following chemical reaction
