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Serine inhibition

Serine inhibits glycerate-3-phosphate-dehy-drogenase, the first reaction in the pathway. [Pg.467]

Inhibitors of cell wall mucopeptide synthesis - The antibiotic O-carbamyl-D-serine is a competitive inhibitor of alanine racemase, whereas D-cyclo-serine inhibits both D-alanyl-D-alanine synthetase and alanine racemase, both enzymes being required for synthesis of the peptide moiety of the mucopeptide 1. ... [Pg.157]

Compounds with functional groups sterically related to threonine and allothreonine, such as serinol and serine inhibited the enzymes differentially. [Pg.93]

Serpins inhibit serine proteinases with a spring-loaded safety catch mechanism... [Pg.110]

Serpins form very tight complexes with their corresponding serine pro-teinases, thereby inhibiting the latter. A flexible loop region of the serpin binds to the active site of the proteinases. Upon release of the serpin from the complex its polypeptide chain is cleaved by the proteinase in the middle of this loop region and the molecule is subsequently degraded. In addition to the active and cleaved states of the serpins there is also a latent state with an intact polypeptide chain that is functionally inactive and does not bind to the proteinase. [Pg.111]

Figure 6.23 Schematic diagram illustrating the active site loop regions (red) in three forms of the serpins. (a) In the active form the loop protrudes from the main part of the molecuie poised to interact with the active site of a serine proteinase. The first few residues of the ioop form a short p strand inserted between ps and pis of sheet A. (h) As a result of inhibiting proteases, the serpin molecules are cleaved at the tip of the active site ioop region, in the cleaved form the N-terminal part of the loop inserts itself between p strands 5 and 15 and forms a long p strand (red) in the middie of the p sheet, (c) In the most stable form, the latent form, which is inactive, the N-terminai part of the ioop forms an inserted p strand as in the cleaved form and the remaining residues form a ioop at the other end of the p sheet. (Adapted from R.W. Carreii et ai., Structure 2 257-270, 1994.)... Figure 6.23 Schematic diagram illustrating the active site loop regions (red) in three forms of the serpins. (a) In the active form the loop protrudes from the main part of the molecuie poised to interact with the active site of a serine proteinase. The first few residues of the ioop form a short p strand inserted between ps and pis of sheet A. (h) As a result of inhibiting proteases, the serpin molecules are cleaved at the tip of the active site ioop region, in the cleaved form the N-terminal part of the loop inserts itself between p strands 5 and 15 and forms a long p strand (red) in the middie of the p sheet, (c) In the most stable form, the latent form, which is inactive, the N-terminai part of the ioop forms an inserted p strand as in the cleaved form and the remaining residues form a ioop at the other end of the p sheet. (Adapted from R.W. Carreii et ai., Structure 2 257-270, 1994.)...
Grtitter, M.G., et al. Crystal structure of the thrombin-hirudin complex a novel mode of serine protease inhibition. EMBO J. 9 2361-2365, 1990. [Pg.220]

FIGURE 5.46 Interaction of the serine hydroxyl residue in the catalytically active site of acetylcholinesterase enzyme with esters of organophosphates or carbamates. The interaction leads to binding of the chemical with the enzyme, inhibition of the enzyme, inhibition of acetylcholine hydrolysis, and thus accumulation of acetylcholine in the synapses. [Pg.287]

Serine proteases like chymotrypsiii are susceptible to inhibition by organic fluorophospbates, such as diisopropyljluorophosphate (DIFP, Figure 16.23). DIFP... [Pg.516]

Cholinesterases (ChEs), polymorphic carboxyles-terases of broad substrate specificity, terminate neurotransmission at cholinergic synapses and neuromuscular junctions (NMJs). Being sensitive to inhibition by organophosphate (OP) poisons, ChEs belong to the serine hydrolases (B type). ChEs share 65% amino acid sequence homology and have similar molecular forms and active centre structures [1]. Substrate and inhibitor specificities classify ChEs into two subtypes ... [Pg.357]

Aspirin has been remarkably successful in the treatment of the pain and swelling of inflammatory disease and in fact, an estimated 45,000 tons of aspirin are still consumed each year. This success resulted in the syntheses of many other aspirin-like drugs , now referred to as NSAIDs. Aspirin, however, continues to have a unique use in the prevention of thrombosis. Since it produces irreversible inhibition of COX-1 by acetylation of serine at position 530 in the active site, a daily low dose of aspirin will cause a cumulative inhibition of COX-1 in platelets, in the portal circulation. A gradual inhibition of platelet aggregation occurs, reducing the possibility of occlusion of coronary or cerebral vessels by platelet thrombi. However, there are no systemic... [Pg.404]


See other pages where Serine inhibition is mentioned: [Pg.27]    [Pg.152]    [Pg.143]    [Pg.380]    [Pg.219]    [Pg.27]    [Pg.152]    [Pg.143]    [Pg.380]    [Pg.219]    [Pg.232]    [Pg.480]    [Pg.45]    [Pg.45]    [Pg.45]    [Pg.467]    [Pg.152]    [Pg.206]    [Pg.391]    [Pg.29]    [Pg.46]    [Pg.454]    [Pg.110]    [Pg.414]    [Pg.468]    [Pg.667]    [Pg.667]    [Pg.106]    [Pg.2]    [Pg.24]    [Pg.430]    [Pg.430]    [Pg.51]    [Pg.71]    [Pg.161]    [Pg.168]    [Pg.172]    [Pg.177]    [Pg.357]    [Pg.360]   
See also in sourсe #XX -- [ Pg.305 ]

See also in sourсe #XX -- [ Pg.75 , Pg.75 ]




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