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Document Figure 3 The main metabolic routes of dopamine and noradrenaline in the brain. COMT, Catechol O-methyltransferase; MAO, monoamino oxidase; DDC, dopa decarboxylase; DBH, dopamine β-hydroxylase; 3-OMD, 3-methoxytyrosine; Dopac, dihydroxyphenyl acetic acid. Page 346 enzyme [13]. The existence of a thermolabile low-activity and a thermostable high-activity COMT in human population has been reported [18]. Interestingly, the two published sequences of human soluble COMT differ in only one amino acid. Recent kinetic studies have shown that this difference affects unambiguously the thermostability of the enzyme [19]. C. Kinetics of Human COMT The kinetic mechanism of the methylation reaction of human COMT has been studied exhaustively using recombinant enzymes [19]. The mechanism is sequential ordered: AdoMet binding first, then Mg 2+ and the catechol substrate as the last ligand. Human S-COMT and MB-COMT have similar kinetic properties. The main difference is the one-order lower K m value of MB-COMT for dopamine as substrate (S-COMT 207 μM and MB-COMT 15 μM). The COMT enzyme is a rather slow enzyme with a low catalytic number. At saturating substrate levels S-COMT has a double efficiency compared with MB-COMT (k cat=37 and k cat =17, respectively). At low substrate concentrations (
Document Figure 4 Amino acid sequence comparison of known COMT sequences (rat [11], human [14], pig [13]). Secondary structure elements in the sequence of rat soluble COMT are indicated as well as important active-site residues involved in binding of ligands (a, AdoMet; m, magnesium; s, substrate/inhibitor). The numbering of the residues corresponds to the soluble enzyme. The extension of the MB-COMT consists of the first 50 amino terminal residues. In the human sequence of COMT determined by Bertocci [13], Val108 is replaced by Met108. Under physiological concentrations of catecholamines in the brain, MB-COMT may play a more important role than S-COMT [19,20]. D. Three-Dimensional Structure of COMT Backbone Page 347 The crystal structure of rat soluble COMT has been solved at 2.0 Å resolution [21]. The COMT enzyme has a single domain α/β-folded structure, in which eight α-helices are arranged around the the central mixed β sheet. The sheet contains five parallel β strands and one antiparallel β hairpin. An overview of COMT is illustrated in Figure 5. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_347.html (1 of 2) [4/5/2004 5:27:50 PM]
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Page 421 and 422: Document Page 343 14 Structural Asp
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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