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Flavin adenine dinucleotide phosphatase

The conversion of riboflavin to flavin mononucleotide (FMN) is catalyzed by flavokinase (Figure 9.73). This conversion may occur during absorption through the gut mucosa or in other organs. The subsequent conversion of FMN to flavin adenine dinucleotide (FAD) is catalyzed by FAD synthase. FAD synthase uses ATP as a source of an adenylyl group, in this conversion (McCormick et ah, 1997). Various phosphatases, including those of the gut mucosa, can catalyze the breakdown of FAD to FMN and of FMN to free riboflavin. Dietary flavins that are covalently botmd to proteins are thought to be unavailable and not to contribute to our dietary needs (Bates et ah, 1997). [Pg.609]

ADP AFP ab as ALAT AP ASAT ATP BQ BSA CEH CK CME COD con A CV d D E E EC ECME EDTA EIA /e FAD FET FIA G GOD G6P-DH HBg HCG adenosine diphosphate a-fetoprotein antibody antigen alanine aminotranferase alkaline phosphatase aspartate aminotransferase adenosine triphosphate benzoquinone bovine serum albumin cholesterol ester hydrolase creatine kinase chemically modified electrode cholesterol oxidase concanavalin A coefficient of variation (relative standard deviation) layer thickness diffusion coefficient enzyme potential Enzyme Classification enzyme-chemically modified electrode ethylene diamine tetraacetic acid enzyme immunoassay enzyme loading factor flavin adenine dinucleotide field effect transistor flow injection analysis amplification factor glucose oxidase glucose-6-phosphate dehydrogenase hepatitis B surface antigen human chorionic gonadotropin... [Pg.327]

Other - Farnesylpyrophosphate synthetase has been used in asymmetric synthesis of isoprenoids. Potato acid phosphatase has been applied to mild hydrolysis of polyprenyl pyrophosphates. Sulfatase-catalyzed hydrolysis of /9-napthol sulfate has been used to separate a- and 8-napthols. NAD and flavin adenine dinucleotide have been made by enzymic coupling reactions. [Pg.268]

The most common forms of vitamin B2 are riboflavin 5 -phosphate (FMN) and flavin adenine dinucleotide (FAD), which are best known for their participation as co-factors (ligands) to some of the enzymes involved in electron transfer chains. The ligand is usually coupled to enzymes through the phosphate moiety and therefore isolation from tissue can be achieved by either mild acid hydrolysis or by enzymatic digestion with an acid phosphatase. [Pg.280]

ACP = acyl carrier protein ACPA D = ACPA desat-urase AlkB = octane 1-monooxygenase AOX = alternative oxidase DMQ hydroxylase = 5-demethoxyquinone hydroxylase EXAFS = extended X-ray absorption fine structure spectroscopy FMN = flavin mononucleotide FprA = flavoprotein A (flavo-diiron enzyme homologue) Hr = hemerythrin MCD = magnetic circular dichroism MME hydroxylase = Mg-protophorphyrin IX monomethyl ester hydroxylase MMO = methane monooxygenase MMOH = hydroxylase component of MMO NADH = reduced nicotinamide adenine dinucleotide PAPs = purple acid phosphatases PCET = proton-coupled electron transfer, PTOX = plastid terminal oxidase R2 = ribonucleotide reductase R2 subunit Rbr = rubrerythrin RFQ = rapid freeze-quench RNR = ribonucleotide reductase ROO = rubredoxin oxygen oxidoreductase XylM = xylene monooxygenase. [Pg.2229]


See other pages where Flavin adenine dinucleotide phosphatase is mentioned: [Pg.611]    [Pg.611]    [Pg.308]    [Pg.62]    [Pg.702]    [Pg.2230]   
See also in sourсe #XX -- [ Pg.595 , Pg.612 ]




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Dinucleotide

Flavin adenine

Flavin adenine dinucleotide

Flavine adenine dinucleotide

Flavines

Flavins

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