Introduction to Enzymes | (S)-limonene 7-monooxygenase of Enzymes
(S)-limonene 7-monooxygenase of enzymesIn enzymology, a (S)-limonene 7-monooxygenase (EC 126.96.36.199) is an enzyme that catalyzes the chemical reaction(-)-(S)-limonene NADPH H O2 displaystyle rightleftharpoons (-)-perillyl alcohol NADP H2OThe 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H, and O2, whereas its 3 products are (-)-perillyl alcohol, NADP, and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common use include (-)-limonene 7-monooxygenase, (-)-limonene hydroxylase, (-)-limonene monooxygenase, and (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.------Preparation of enzymesThrough a cut in the throat, the gills and part of the gullet are removed from the herring, eliminating any bitter taste. The liver and pancreas are left in the fish during the salt-curing process because they release enzymes essential for flavor. The herrings are then placed in the brine for approximately 5 days, traditionally in oak casks. They require no further preparation after fillet and skin removal and can be eaten as a snack with finely sliced raw onion and pickles.As skin removal requires experience, fillets or double fillets should be attempted first. The soused herrings are silvery outside and pink inside when fresh, and should not be bought if they appear grey and oily.Whereas salt herrings have a salt content of 20% and must be soaked in water before consumption, soused herrings do not need soaking.------Nudix hydrolase of enzymesNudix hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x (any moiety), hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the Nudix superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.There are two components to the Nudix family: the so-called Nudix fold of a beta sheet with alpha helices on each side and the Nudix motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is isoleucine, leucine or valine, and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids. Nudix hydrolases include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A hydrolases, RppH, and many others.------Benzoate 4-monooxygenase of enzymesIn enzymology, a benzoate 4-monooxygenase (EC 188.8.131.52) is an enzyme that catalyzes the chemical reactionbenzoate NADPH H O2 displaystyle rightleftharpoons 4-hydroxybenzoate NADP H2OThe 4 substrates of this enzyme are benzoate, NADPH, H, and O2, whereas its 3 products are 4-hydroxybenzoate, NADP, and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use include benzoic acid 4-hydroxylase, benzoate 4-hydroxylase, benzoic 4-hydroxylase, benzoate-p-hydroxylase, and p-hydroxybenzoate hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: iron, Tetrahydrobiopterin, and Tetrahydropteridine.------ADAMTS of enzymesADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes. 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan, making them key remodeling enzymes of the extracellular matrix. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described. Most cases of thrombotic thrombocytopenic purpura arise from autoantibody-mediated inhibition of ADAMTS13.Like ADAMs, the name of the ADAMTS family refers to its disintegrin and metalloproteinase activity, and in the case of ADAMTS, the presence of a thrombospondin motif.------Research of enzymesNagaraja has done research on DNA topoisomerases, topology modulation, regulation of gene expression to understand the underlying molecular mechanisms and their importance in cellular function. Understanding the biology of the pathogen that causes TB has been a major research effort. As a result, several seminal contributions have been made leading to potential applications. His interaction with industry includes development of commercial biotech products such as restriction enzymes and other DNA transaction enzymes, design and development of high fidelity restriction enzyme, new inhibitors for the generation of lead molecules as a step for novel therapeutics against tuberculosis. These have been successfully applied and resulted in international patents. Under his guidance, 21 students have completed doctoral degree and 10 students are at various stages of their PhD. In addition, a large number of project assistants, summer fellows and postdoctoral researchers are trained under him------Identity of hepoxilin-epoxide hydrolase of enzymesRecent studies have shown that Soluble epoxide hydrolase (i.e. epoxide hydrolase 2 or EH2) readily metabolizes a) hepoxilin A3 (8-hydroxy-11S,12Sepoxy-(5Z,8Z,14Z)-eicosatrienoic acid) to trioxilin A3 (8,11,12-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid) and b) hepoxilin B3 (10-hydroxy-11S,12Sepoxy-(5Z,9E,14Z)-eicosatrienoic acid) to trioxlin B3 (10,11,12-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid. Soluble epoxide hydrolase (i.e. epoxide hydrolase 2 or EH2) sEH also appears to be the hepoxilin hydrolase that is responsible for inactivating the epoxyalcohol metabolites of arachidonic acid, hepoxilin A3 and hepoxiin B3. Soluble epoxide hydrolase is widely expressed in a diversity of human and other mammal tissues and therefore appears to be the hepoxilin hydrolase responsible for inactivating hepoxilin A3 and B3 (see soluble epoxide hydrolase#Function and epoxide hydrolase#Hepoxilin-epoxide hydrolase). The ability of EH1, EH3, EH4, and leukotriene A4 hydrolase to metabolize hepoxilins to trioxilins has not yet been reported------ATP10 protein of enzymesIn molecular biology, ATP10 protein (mitochondrial ATPase complex subunit ATP10) is an ATP synthase assembly factor. It is essential for the assembly of the mitochondrial F1-F0 complex. A yeast nuclear gene (ATP10) encodes a product that is essential for the assembly of a functional mitochondrial ATPase complex. Mutations in ATP10 induce a loss of rutamycin sensitivity in the mitochondrial ATPase, but do not affect the respiratory enzymes. ATP10 has a molecular weight of 30,293 Da and its primary structure is not related to any known subunit of the yeast or mammalian mitochondrial ATPase complexes. ATP10 is associated with the mitochondrial membrane. It is suggested that the ATP10 product is not a subunit of the ATPase complex but rather a protein required for the assembly of the F0 sector of the complex.------Indications of enzymesAs with all prescription veterinary medicine, advice on the use of pradofloxacin should always be sought from a suitably qualified veterinarian.DogsIn Europe Pradofloxacin is indicated for the treatment of:wound infections and superficial and deep pyoderma caused by susceptible strains of the Staphylococcus intermedius group (including S. pseudintermedius),acute urinary tract infections caused by susceptible strains of Escherichia coli and the Staphylococcus intermedius group (including S. pseudintermedius) andas adjunctive treatment to mechanical or surgical periodontal therapy in the treatment of severe infections of the gingiva and periodontal tissues caused by susceptible strains of anaerobic organisms, for example Porphyromonas spp. and Prevotella spp.CatsPradofloxacin is indicated for the treatment of:acute infections of the upper respiratory tract caused by susceptible strains of Pasteurella multocida, Escherichia coli and the Staphylococcus intermedius group (including S. pseudintermedius).wound infections and abscesses caused by susceptible strains of Pasteurella multocida and the Staphylococcus intermedius group (including S. pseudintermedius) for oral suspension only.------Glycoside hydrolase family 18 of enzymesIn molecular biology, Glycoside hydrolase family 18 is a family of glycoside hydrolases.Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Some members of this family, CAZY GH_18, belong to the chitinase class II group which includes chitinase, chitodextrinase and the killer toxin of Kluyveromyces lactis. The chitinases hydrolyse chitin oligosaccharides. Another chitinase II member is the novel gene Chitinase domain-containing protein 1. The family also includes various glycoproteins from mammals; cartilage glycoprotein and the oviduct-specific glycoproteins are two examples.------UDP-sulfoquinovose synthase of enzymesUDP-sulfoquinovose synthase (EC 184.108.40.206) is an enzyme that catalyzes the chemical reactionUDP-glucose sulfite displaystyle rightleftharpoons UDP-6-sulfoquinovose H2OThus, the two substrates of this enzyme are UDP-glucose and sulfite, whereas its two products are UDP-6-sulfoquinovose and H2O.In a subsequent reaction catalyzed by sulfoquinovosyl diacylglycerol synthase, the sulfoquinovose portion of UDP-sulfoquinovose is combined with diacyglycerol to produce the sulfolipid sulfoquinovosyl diacylglycerol (SQDG).This enzyme belongs to the family of hydrolases, specifically those acting on carbon-sulfur bonds. The systematic name of this enzyme class is UDP-6-sulfo-6-deoxyglucose sulfohydrolase. Other names in common use include sulfite:UDP-glucose sulfotransferase, and UDP-sulfoquinovose synthase. This enzyme participates in nucleotide sugars metabolism and glycerolipid metabolism.The 3-dimensional structure of the enzyme is known from Protein Data Bank entries 1qrr (Mulichak et al., 1999), 1i24, 1i2b and 1i2c.------Diagnosis of enzymesTypesHyperprolinemia type IIt is difficult to determine the prevalence of hyperprolinemia type I, as many people with the condition are asymptomatic.People with hyperprolinemia type I have proline levels in their blood between 3 and 10 times the normal level. Some individuals with type I exhibit seizures, intellectual disability, or other neurological problems.Hyperprolinemia type IIHyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate. This rare form of the disorder may appear benign at times, but often involves seizures, convulsions, and intellectual disability.Hyperprolinemia can also occur with other conditions, such as malnutrition or liver disease. In particular, individuals with conditions that cause elevated levels of lactic acid in the blood, such as lactic acidemia, are likely to have elevated proline levels, because lactic acid inhibits the breakdown of proline.------Isoflavone 2'-hydroxylase of enzymesIn enzymology, an isoflavone 2'-hydroxylase (EC 220.127.116.11) is an enzyme that catalyzes the chemical reactionan isoflavone NADPH H O2 displaystyle rightleftharpoons a 2'-hydroxyisoflavone NADP H2OThe 4 substrates of this enzyme are isoflavone, NADPH, H, and O2, whereas its 3 products are 2'-hydroxyisoflavone, NADP, and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase, CYP81E1, and CYP Ge-3. This enzyme participates in isoflavonoid biosynthesis.