Short hydrogen bonds in the catalytic mechanism of serine proteases
| Autor: | Leskovac Vladimir, Trivić Svetlana, Peričin Draginja, Popović Mira, Kandrač Julijan |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: | |
| Zdroj: | Journal of the Serbian Chemical Society, Vol 73, Iss 4, Pp 393-403 (2008) |
| Druh dokumentu: | article |
| ISSN: | 0352-5139 1820-7421 |
| DOI: | 10.2298/JSC0804393L |
| Popis: | The survey of crystallographic data from the Protein Data Bank for 37 structures of trypsin and other serine proteases at a resolution of 0.78-1.28 Å revealed the presence of hydrogen bonds in the active site of the enzymes, which are formed between the catalytic histidine and aspartate residues and are on average 2.7 Å long. This is the typical bond length for normal hydrogen bonds. The geometric properties of the hydrogen bonds in the active site indicate that the H atom is not centered between the heteroatoms of the catalytic histidine and aspartate residues in the active site. Taken together, these findings exclude the possibility that short "low-barrier" hydrogen bonds are formed in the ground state structure of the active sites examined in this work. Some time ago, it was suggested by Cleland that the "low-barrier hydrogen bond" hypothesis is operative in the catalytic mechanism of serine proteases, and requires the presence of short hydrogen bonds around 2.4 Å long in the active site, with the H atom centered between the catalytic heteroatoms. The conclusions drawn from this work do not exclude the validity of the "low-barrier hydrogen bond" hypothesis at all, but they merely do not support it in this particular case, with this particular class of enzymes. |
| Databáze: | Directory of Open Access Journals |
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