In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide: Thus, the two substrates of this enzyme are monocarboxylic acid amide and H2O, whereas its two products are monocarboxylate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation. Amidases contain a conserved stretch of approximately 130 ...

In enzymology, a hippurate hydrolase (EC 3.5.1.32) is an enzyme that catalyzes the chemical reaction hippurate + H2O ⇌ {\displaystyle \rightleftharpoons } benzoate + glycine Thus, the two substrates of this enzyme are hippurate and H2O, whereas its two products are benzoate and glycine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzoylamino-acid amidohydrolase. This enzyme participates in phenylalanine metabolism. Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH (2006). "Sonographic measurement of cervical length and fetal fibronectin testing in threatened preterm labor". Ultrasound. Obstet. Gynecol. 27 (4): 368-72. doi:10.1002/uog.2723. PMID 16526097. Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH (2006). "Sonographic measurement of cervical length and fetal fibronectin testing in threatened preterm labor". Ultrasound. ...

... (INN) or monosulfiram, trade name Tetmosol, is an ectoparasiticide used in the treatment and prevention of scabies. It is usually sold as a solution or medicated soap, sometimes in combination with benzyl benzoate. Sulfiram is now rarely used, but, as of 2015[update], is still available in Brazil, India, and South Africa (as monotherapy). Dizziness, headache, fatigue and erythematous rash may occur. A single case of toxic epidermal necrolysis was reported in 1968. Sulfiram is structurally related to disulfiram (Antabuse), and readily converts to disulfiram when exposed to light. Like disulfiram, it can produce an unpleasant reaction when consumed with alcohol. Sweetman, Sean C., ed. (2009). "Pesticides and repellents". Martindale: the complete drug reference (36th ed.). London: Pharmaceutical Press. p. 2050. ISBN 978-0-85369-840-1. [No authors listed] (2009). "Sarfiram - Bula". Bulário de Remédios Comerciais (in Portuguese). MedicinaNET. Retrieved 2010-08-11. Copeman PW (March 1968). ...

... (FMO3), also known as dimethylaniline monooxygenase [N-oxide-forming] 3 and trimethylamine monooxygenase, is a flavoprotein enzyme (EC 1.14.13.148) that in humans is encoded by the FMO3 gene. This enzyme catalyzes the following chemical reaction: N,N,N-trimethylamine + NADPH + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } N,N,N-trimethylamine N-oxide + NADP+ + H2O FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. The human FMO3 enzyme catalyzes several types of reactions, including: the N-oxygenation of primary, secondary, and tertiary amines; the S-oxygenation of nucleophilic sulfur-containing compounds; and the 6-methylhydroxylation of DMXAA. FMO3 is the primary enzyme in humans which catalyzes the N-oxidation of trimethylamine into trimethylamine N-oxide; FMO1 also N-oxygenates trimethylamine, but to a much lesser extent than FMO3. Genetic deficiencies of the FMO3 enzyme cause primary ...

... (also called squalene epoxidase) is an enzyme that uses NADPH and molecular oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway. In humans, squalene epoxidase is encoded by the SQLE gene. Squalene monooxygenase (SqMO) was formerly referred to as squalene epoxidase (SqE) in the literature. Squalene monooxygenase is a flavoprotein monooxygenase. Flavoprotein monooxygenase form flavin hydroperoxides at the enzyme active site, which then transfer the terminal oxygen atom of the hydroperoxide to the substrate. Squalene monooxygenase differs from other flavin monooxygenases in that the oxygen is inserted as an epoxide rather than as a hydroxyl group. Squalene monooxygenase contains a loosely bound FAD flavin and obtains electrons ...

The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group. FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals. These monooxygenases are often misclassified because they share activity profiles similar to those of cytochrome P450 (CYP450), which is the major contributor to oxidative xenobiotic metabolism. However, a key difference ...

A styrene monooxygenase (SMO; EC 1.14.14.11) is an enzyme that catalyzes the chemical reaction styrene + FADH2 + O2 ↔ (S)-2-phenyloxirane + FAD + H2O as the first step of the aerobic styrene degradation pathway. The product 2-phenyloxirane is also known as styrene oxide and can be converted by a styrene oxide isomerase (SOI) to obtain phenylacetaldehyde, which can be transformed into the key-intermediate phenylacetic acid by a phenylacetaldehyde dehydrogenase (PAD). The enzyme belongs to the group of oxidoreductases according EC classification and is dependent on FAD as cofactor, thus it was classified as an external flavoprotein monooxygenase (designated as type E). It forms a two-component system with a reductase (StyB, StyA2B). The reductase utilizes solely NADH to reduce the FAD, which is then transferred to the styrene monooxygenase (StyA, StyA1). Two types of that enzyme are described so far: StyA/StyB (designated E1), first described from Pseudomonas ...

... (EC 1.14.14.9) is an enzyme that catalyzes the chemical reaction 4-hydroxyphenylacetate + FADH2 + O2 ⇌ {\displaystyle \rightleftharpoons } 3,4-dihydroxyphenylacetate + FAD + H2O This reaction is the first step in a pathway found in enteric bacteria such as Escherichia coli and soil bacteria such as Pseudomonas putida which degrades 4-hydroxyphenylacetate (4-HPA), allowing these bacteria to use 4-HPA and other aromatic compounds found in mammalian digestive tracts or in soil as a carbon source. While most known flavin monooxygenases use NADH or NADPH as substrates (and use the flavins FAD or FMN as prosthetic groups ), this enzyme is part of a two-component system, in which a flavin oxidoreductase partner (EC 1.5.1.37) regenerates FADH2 by oxidizing NADH to NAD+. hpaB and hpaC, the 4-HPA oxygenase and reductase partner proteins (respectively) of E. coli strain W, were the first two-component flavin monoxygenase system identified. While known examples of ...

Neutrophil cytosol factor 4 is a protein that in humans is encoded by the NCF4 gene. The protein encoded by this gene is a cytosolic regulatory component of the superoxide-producing phagocyte NADPH-oxidase, a multicomponent enzyme system important for host defense. This protein is preferentially expressed in cells of myeloid lineage. It interacts primarily with neutrophil cytosolic factor 2 (NCF2/p67-phox) to form a complex with neutrophil cytosolic factor 1 (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex then activates flavocytochrome b, the membrane-integrated catalytic core of the enzyme system. The PX domain of this protein can bind phospholipid products of the PI(3) kinase, which suggests its role in PI(3) kinase-mediated signaling events. The phosphorylation of this protein was found to negatively regulate the enzyme activity. Alternatively spliced transcript variants encoding distinct isoforms have ...

In enzymology, a hydroperoxide dehydratase (EC 4.2.1.92) is an enzyme that catalyzes the chemical reaction (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate ⇌ {\displaystyle \rightleftharpoons } (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate + H2O Hence, this enzyme has one substrate, (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate, and two products, (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]. Other names in common use include hydroperoxide isomerase, linoleate hydroperoxide isomerase, linoleic acid hydroperoxide isomerase, HPI, (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate, and 12,13-hydro-lyase. As of late 2007, only one structure has been solved for this class of enzymes, with ...

... (SPM, also termed specialized proresolving mediators) are a large and growing class of cell signaling molecules formed in cells by the metabolism of polyunsaturated fatty acids (PUFA) by one or a combination of lipoxygenase, cyclooxygenase, and cytochrome P450 monooxygenase enzymes. Pre-clinical studies, primarily in animal models and human tissues, implicate SPM in orchestrating the resolution of inflammation. SPM join the long list of other physiological agents which tend to limit inflammation (see Inflammation § Resolution of inflammation) including glucocorticoids, interleukin 10 (an anti-inflammatory cytokine), interleukin 1 receptor antagonist (an inhibitor of the action of pro-inflammatory cytokine, interleukin 1), annexin A1 (an inhibitor of formation of pro-inflammatory metabolites of polyunsaturated fatty acids), and the gaseous resolvins, carbon monoxide (see Carbon monoxide § Normal human physiology), nitric oxide (see Nitric oxide § Biological ...

... s (sometimes called methanophiles) are prokaryotes that metabolize methane as their only source of carbon and energy. They can grow aerobically or anaerobically and require single-carbon compounds to survive. These Methanotrophs are currently being modified to absorb methane from the atmosphere, because methane released into the atmosphere contributes to greenhouse gasses, which heat up the earth and cause global warming. Under aerobic conditions, they combine oxygen and methane to form formaldehyde, which is then incorporated into organic compounds via the serine pathway or the ribulose monophosphate (RuMP) pathway. Type I methanotrophs are part of the Gammaproteobacteria and they use the RuMP pathway to assimilate carbon. Type II methanotrophs are part of the Alphaproteobacteria and utilize the Serine pathway of carbon assimilation. They also characteristically have a system of internal membranes within which methane oxidation occurs. Methanotrophs occur mostly in soils, and are ...

Saito, K., Kobayashi, M., Gong, Z., Tanaka, Y. and Yamazaki, M. (1999). "Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens". Plant J. 17: 181-190. PMID 10074715. ...