EC Number |
General Information |
Reference |
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3.4.22.70 | malfunction |
deficiency of srtA impairs the release of pro-inflammatory cytokines in Staphylococcus aureus-induced mastitis. A DEKTASrtA mutant strain attenuates the inflammatory reaction in the mammary tissue of mice compared with wild-type Staphylococcus aureus challenge. The enzyme mutant strain impairs the induction of pro-inflammatory cytokines such as tumor necrosis factor-alpha, interleukin-1beta, and interleukin-6, the mutant strain blocks the activation of nuclear factor kappaB and mitogen-activated protein kinases by attenuating the degradation and phosphorylation of signaling pathway molecules such as IkappaBalpha, p65 and p38. |
-, 731825 |
3.4.22.70 | malfunction |
deletion of srtA affects the attachment stage and results in a deficiency in biofilm production, deletion of srtA has no effect on cell viability and cell growth |
708707 |
3.4.22.70 | malfunction |
the deletion of sortase A affects the virulence and infectious capacity of Streptococcus iniae |
-, 731833 |
3.4.22.70 | more |
binding mechanism is a conformational selection followed by induced fit, and allosteric regulation of the enzyme, molecular dynamics simulations of the enzyme in apo state and when bound to an LPATG sorting signal, which adopts multiple metastable states, overview. The first and the second substrate binding sites are proposed to be located on opposing faces of the protein. The active sites of all sortases contain a conserved catalytic triad that consists of residues H120, C184, and R197. NMR SrtA structure covalently bound to a modified sorting signal, binding conformations, overview |
732881 |
3.4.22.70 | more |
during catalysis sortase A cleaves the conserved Leu-Pro-X-Thr-Gly sorting motif at the Thr residue under concomitant thioester formation at active site Cys184, mechanism, overview |
731485 |
3.4.22.70 | more |
sortase A mediates site-specific immobilization for identification of protein interactions in affinity purification-mass spectrometry experiments, overview |
732898 |
3.4.22.70 | more |
substrate-induced conformational dynamics in the enzyme, roles of invariant Leu and Pro residues of the substrate in modulating the enzyme dynamics, analysis of the selection process of a catalytically competent substrate, molecular dynamics simulations with noncanonical substrates, overview. The linked conformation due to Pro in LPXTG is obligatory for productive binding but does not per se control the enzyme dynamics. The Leu residue of the substrate appears to play the crucial role of an anchor to the beta6-beta7 loop directing the conformational transition of the enzyme from an open to a closed state subsequent to which the Pro residue facilitates the consummation of binding through predominant engagement of the loop and catalytic motif residues in hydrophobic interactions, molecular dynamics simulations, overview |
731314 |
3.4.22.70 | more |
the structural integrity of circular sortase A and its biochemical characteristics are compared to those of the linear enzyme analog and are similar under native conditions, overview. Circular enzyme is active at concentrations of urea up to 3 M and is capable of efficient catalytic protein-protein coupling, while the linear enzyme is unable to mediate the ligation of substrate proteins under the same conditions |
-, 731266 |
3.4.22.70 | physiological function |
as a transpeptidase that covalently attaches various virulence factors to the cell surface, this enzyme plays a crucial role in the ability of bacteria to invade the host's tissues and to escape the immune response |
731478 |
3.4.22.70 | physiological function |
Bacillus anthracis uses the sortase A enzyme to anchor proteins to its cell wall envelope during vegetative growth |
709123 |