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Content Provider | Journal of Biological Chemistry (JBC) |
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Author | Bömmel, Heike M. Reif, Andreas Fröhlich, Lothar G. Frey, Armin Hofmann, Heinrich Marecak, Dale M. Groehn, Viola Kotsonis, Peter La, Mylinh Köster, Sandra Meinecke, Matthias Bernhardt, Manfred Weeger, Monika Ghisla, Sandro Prestwich, Glenn D. Pfleiderer, Wolfgang Schmidt, Harald H. H. W. |
Abstract | Nitric oxide synthases (NOS) are homodimeric enzymes that NADPH-dependently convertl-arginine to nitric oxide andl-citrulline. Interestingly, all NOS also require (6R)-5,6,7,8-tetrahydro-l-biopterin (H4Bip) for maximal activity although the mechanism is not fully understood. Basal NOS activity, i.e. that in the absence of exogenous H4Bip, has been attributed to enzyme-associated H4Bip. To elucidate further H4Bip function in purified NOS, we developed two types of pterin-based NOS inhibitors, termed anti-pterins. In contrast to type II anti-pterins, type I anti-pterins specifically displaced enzyme-associated H4Bip and inhibited H4Bip-stimulated NOS activity in a fully competitive manner but, surprisingly, had no effect on basal NOS activity. Moreover, for a number of different NOS preparations basal activity (percent ofV max) was frequently higher than the percentage of pterin saturation and was not affected by preincubation of enzyme with H4Bip. Thus, basal NOS activity appeared to be independent of enzyme-associated H4Bip. The lack of intrinsic 4a-pterincarbinolamine dehydratase activity argued against classical H4Bip redox cycling in NOS. Rather, H4Bip was required for both maximal activity and stability of NOS by binding to the oxygenase/dimerization domain and preventing monomerization and inactivation duringl-arginine turnover. Since anti-pterins were also effective in intact cells, they may become useful in modulating states of pathologically high nitric oxide formation. |
Related Links | http://www.jbc.org/content/273/50/33142.abstract |
Ending Page | 33149 |
Starting Page | 33142 |
Page Count | 8 |
File Format | HTM / HTML PDF |
ISSN | 00219258 |
Journal | Journal of Biological Chemistry (JBC) |
Issue Number | 50 |
Volume Number | 273 |
DOI | 10.1074/jbc.273.50.33142 |
e-ISSN | 1083351X |
Language | English |
Publisher | American Society for Biochemistry and Molecular Biology |
Publisher Date | 1998-12-11 |
Access Restriction | Open |
Subject Keyword | Nitric oxide (NO) 3-[(3-cholamidopropyl)-imethylammonio]-2-hydroxy-1-propansulfonate (CHAPSO) Dihydrobiopterin (H2Bip) 5,6,7,8-l-tetrahydro-l-biopterin (H4Bip) Dihydro-pterin (H2Pte) Tetrahydro-pterin (H4Pte) NOS-I N terminus + oxygenase domain (N+ NOSox) NO synthase (NOS) Basally active NOS (NOS*) Basally inactive NOS (NOS°) NOS-I oxygenase domain (NOSox) NOS-I reductase domain (NOSred) Pterin-4a-carbinolamine dehydratase (PCD) Anti-pterin code number (PHS) Pterin (Pte) Quinoid-H2Bip (q-H2Bip) Triethanolamine. (TEA) ENZYMOLOGY |
Content Type | Text |
Resource Type | Article |
Subject | Molecular Biology Cell Biology Biochemistry |
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