Please use this identifier to cite or link to this item:
https://open.uns.ac.rs/handle/123456789/9916
DC Field | Value | Language |
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dc.contributor.author | Leskovac V. | en |
dc.contributor.author | Trivic S. | en |
dc.contributor.author | Peričin D. | en |
dc.contributor.author | Popović M. | en |
dc.contributor.author | Kandrač J. | en |
dc.date.accessioned | 2020-03-03T14:35:55Z | - |
dc.date.available | 2020-03-03T14:35:55Z | - |
dc.date.issued | 2008-04-01 | en |
dc.identifier.issn | 03525139 | en |
dc.identifier.uri | https://open.uns.ac.rs/handle/123456789/9916 | - |
dc.description.abstract | 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. | en |
dc.relation.ispartof | Journal of the Serbian Chemical Society | en |
dc.title | Short hydrogen bonds in the catalytic mechanism of serine proteases | en |
dc.type | Journal/Magazine Article | en |
dc.identifier.doi | 10.2298/JSC0804393L | en |
dc.identifier.scopus | 2-s2.0-42349110780 | en |
dc.identifier.url | https://api.elsevier.com/content/abstract/scopus_id/42349110780 | en |
dc.relation.lastpage | 403 | en |
dc.relation.firstpage | 393 | en |
dc.relation.issue | 4 | en |
dc.relation.volume | 73 | en |
item.grantfulltext | none | - |
item.fulltext | No Fulltext | - |
Appears in Collections: | TF Publikacije/Publications |
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