- SASDB35: Staphylococcus aureus thiaminase II (Thiaminase type II enzyme, S... -
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Basic information
Entry
Database: SASBDB / ID: SASDB35
Sample
Staphylococcus aureus thiaminase II
Thiaminase type II enzyme (protein), SaTenA, Staphylococcus aureus
Function / homology
aminopyrimidine aminohydrolase / Thiaminase II / thiaminase activity / Thiaminase-2/PQQC / TENA/THI-4/PQQC family / thiamine diphosphate biosynthetic process / Haem oxygenase-like, multi-helical / thiamine biosynthetic process / Aminopyrimidine aminohydrolase
Function and homology information
Biological species
Staphylococcus aureus (bacteria)
Citation
Journal: Acta Crystallogr D Biol Crystallogr / Year: 2013 Title: Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases. Authors: Afshan Begum / Julia Drebes / Alexey Kikhney / Ingrid B Müller / Markus Perbandt / Dmitri Svergun / Carsten Wrenger / Christian Betzel / Abstract: Staphylococcus aureus TenA (SaTenA) is a thiaminase type II enzyme that catalyzes the deamination of aminopyrimidine, as well as the cleavage of thiamine into 4-amino-5-hydroxymethyl-2- ...Staphylococcus aureus TenA (SaTenA) is a thiaminase type II enzyme that catalyzes the deamination of aminopyrimidine, as well as the cleavage of thiamine into 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine (vitamin B1) metabolism. Further, by analogy with studies of Bacillus subtilis TenA, SaTenA may act as a regulator controlling the secretion of extracellular proteases such as the subtilisin type of enzymes in bacteria. Thiamine biosynthesis has been identified as a potential drug target of the multi-resistant pathogen S. aureus and therefore all enzymes involved in the S. aureus thiamine pathway are presently being investigated in detail. Here, the structure of SaTenA, determined by molecular replacement and refined at 2.7 Å resolution to an R factor of 21.6% with one homotetramer in the asymmetric unit in the orthorhombic space group P212121, is presented. The tetrameric state of wild-type (WT) SaTenA was postulated to be the functional biological unit and was confirmed by small-angle X-ray scattering (SAXS) experiments in solution. To obtain insights into structural and functional features of the oligomeric SaTenA, comparative kinetic investigations as well as experiments analyzing the structural stability of the WT SaTenA tetramer versus a monomeric SaTenA mutant were performed.
Contact author
Al Kikhney (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)
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