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Activator, transferase

The secondary or tertiary structure can prevent glyco-sylation of sites within those regions, and disruption of tertiary structure allows glycosylation to occur at new sites in certain glycoproteins. Availability of active transferase and of lipid-linked oligosaccharide also affects the rate of glycosylation. [Pg.315]

The chemistry of complex lipids is dominated by regioselective hydrolysis reactions of (1) the glyceryl fatty acid esters and (2) phosphate diesters. Both types of reactions are routinely performed with the corresponding esterases. A large variety of lipid active transferase enzymes is also commercially available. Phospholipases Aj, A, C, and D, for example, split any of the four ester bonds of a phospholipid regioselectively. The product without a fatty acid side chain at C2 of glycerol is called a lysophospholipid. Lecithin-cholesterol-acyltransferase transfers the fatty acid at C2, often linoleic acid, to the OH group at C3 of cho-... [Pg.92]

The dependence of glucoso-6-phosphatase activity upon its interaction with membranes has been clearly demonstrated. This enzyme is located on the membranes of the smooth and rough endoplasmic reticulum and remains associated with isolated microsomes. This multifunctional enzyme demonstrated glucoso-6-phosphohydrolase activity (hydrolase) and pyrophosphate glucosophosphotrans-ferase activity (transferase) ... [Pg.94]

Vanadium. Vanadium is essential in rats and chicks (85,156). Estimated human intake is less than 4 mg/d. In animals, deficiency results in impaired growth, reproduction, and Hpid metaboHsm (157), and altered thyroid peroxidase activities (112). The levels of coen2yme A and coen2yme Q q in rats are reduced and monoamine oxidase activity is increased when rats are given excess vanadium (157). Vanadium may play a role in the regulation of (NaK)—ATPase, phosphoryl transferases, adenylate cyclase, and protein kinases (112). [Pg.388]

Dopamine. Dopamine (DA) (2) is an intermediate in the synthesis of NE and Epi from tyrosine. DA is localized to the basal ganglia of the brain and is involved in the regulation of motor activity and pituitary hormone release. The actions of DA are terminated by conversion to dihydroxyphenylacetic acid (DOPAC) by monoamine oxidase-A and -B (MAO-A and -B) in the neuron following reuptake, or conversion to homovanillic acid (HVA) through the sequential actions of catechol-0-methyl transferase (COMT) and MAO-A and -B in the synaptic cleft. [Pg.540]

Aminohexose Nucleosides. The 4-aminohexose nucleosides (128—140) are Hsted in Table 7 (1—4,240—242). A biosynthetic relationship between the 4-aminohexose peptidyl nucleoside antibiotics and the pentopyranines has been proposed (1). The 4-aminohexose pyrimidine nucleoside antibiotics block peptidyl transferase activity and inhibit transfer of amino acids from aminoacyl-tRNA to polypeptides. Hikizimycin, gougerotin, amicetin, and blasticidin S bind to the peptidyl transferase center at overlapping sites (243). [Pg.129]

Farnesyl transferase from rat cells is a heterodimer consisting of a 48 kD u-snbnnit and a 46 kD /3-snbnnit. In the structure shown here, helices 2 to 15 of the u-snbnnit are folded into seven short coiled coils that together form a crescent-shaped envelope partially surrounding the /3-snbnnit. Twelve helices of the /3-snl> nnit form a novel barrel motif that creates the active site of the enzyme. Farnesyl transferase inhibitors, one of which is shown here, are potent suppressors of tumor growth in mice, but their value in humans has not been established. [Pg.278]

FIGURE 25.10 Acetyl units are covalently linked to a serine residue at the active site of the acetyl transferase in eukaryotes. A similar reaction links malonyl units to the malonyl transferase. [Pg.812]

Consider the role of the pantothenic acid groups in animal fatty acyl synthase and the size of the pantothenic acid group itself, and estimate a maximal separation between the malonyl transferase and the ketoacyl-ACP synthase active sites. [Pg.850]

Application of the desired biotransformation to give a practical and economical process required high molar conversion yields, high amino transferase activities, highly effident product recovery and an inexpensive source of phenylpyruvic add. With genetic and/or biochemical manipulation considerable progress can be made towards meeting some of these requirements. [Pg.268]

Clock gene and transcription factor with histone acetyl-transferase (HAT) activity that (in complex with BMAL1) constitutes a positive limb of molecular circadian oscillators. [Pg.374]

The exact role of individual histone acetylations will have to be determined in the context of other modifications and the number of lysine residues effected. However, the general importance of histone acetylation as a regulator for chromatin activity is undisputed. This leads to the intriguing possibility to develop drugs that target histone acetylation for therapeutic purposes. The primary targets for drug development are the histone acetyl transferases (HATs) and the histone deacetylases (HDACs) which introduce and remove histone acetylations [2, 3]. [Pg.594]

Macrolides are a group of antibiotics, produced in nature by many actinomycetes strains, that are composed of a 12- to 16-membered lactone ring, to which one or more sugar substituents is attached. They target the peptidyl transferase center on the 50S ribosomal subunit and function primarily by interfering with movement of the nascent peptide away from the active site and into the exit tunnel. [Pg.739]

Glutathione S-transferase M1 Deficient activity in about 50% of Caucasians. Carriers of the deficiency may have a slightly increased risk for a number of smoking-related cancers. [Pg.950]

The steps in the subsequent utilization of muscle LCFAs may be summarized as follows. The free fatty acids, liberated from triglycerides by a neutral triglyceride lipase, are activated to form acyl CoAs by the mediation of LCFAcyl-CoA synthetase which is situated on the outer mitochondrial membrane. The next step involves carnitine palmitoyl transferase I (CPT I, see Figure 9) which is also located on the outer mitochondrial membrane and catalyzes the transfer of LCFAcyl residues from CoA to carnitine (y-trimethyl-amino-P-hydroxybutyrate). LCFAcyl... [Pg.303]

Activities of glutamate-pyruvate transaminase (SGPT, GPT) (EC 2.6.1.2), L-y -glutamyl-transferase (y-GT) (EC 2.3.2.2) and level of triglycerides (TG) in serum, as well as levels of glutathione (GSH) and malondialdehyde (MDA) in the liver were determined. [Pg.390]

Gamma-glutamyl-transferase activity was determined according to "Monotest 10 y-GT neu" from Boehringer-Mannheim. [Pg.390]

Polidoro G, Dillio C, Arduini A, et al. 1982. Glutathione peroxidase and glutathione S-transferase activities in human fetal tissues. Inability of acidic forms of glutathione S-transferase to catalyze the reduction of organic hydroperoxides. Biochem Int 4 637-645. [Pg.226]

Emphasis is given to the critical role of metabolism, both detoxication and activation, in determining toxicity. The principal enzymes involved are described, including monooxygenases, esterases, epoxide hydrolases, glutathione-5 -transferases, and glucuronyl transferases. Attention is given to the influence of enzyme induction and enzyme inhibition on toxicity. [Pg.64]


See other pages where Activator, transferase is mentioned: [Pg.595]    [Pg.1361]    [Pg.265]    [Pg.213]    [Pg.119]    [Pg.595]    [Pg.1361]    [Pg.265]    [Pg.213]    [Pg.119]    [Pg.113]    [Pg.44]    [Pg.524]    [Pg.515]    [Pg.65]    [Pg.290]    [Pg.511]    [Pg.103]    [Pg.103]    [Pg.456]    [Pg.811]    [Pg.221]    [Pg.149]    [Pg.594]    [Pg.681]    [Pg.711]    [Pg.898]    [Pg.937]    [Pg.1282]    [Pg.1295]    [Pg.214]    [Pg.200]    [Pg.299]    [Pg.405]    [Pg.84]    [Pg.43]   
See also in sourсe #XX -- [ Pg.153 ]




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Biotinyl transferase activity

Carnitine palmitoyl transferase activity

Carnitine palmitoyl transferase activity towards eicosapentaenoyl- and

Glucuronyl transferase activity

Glutathione transferase, activity

Glutathione-S-transferases activity

Peptidyl transferase activity

The transferase activity of a-galactosidase

Transferase activity

Transferase activity, alkaline phosphatase

Transferases glutathione activity, insects

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