Penicillin acylase

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Current revision (10:51, 5 December 2021) (edit) (undo)
 
Line 24: Line 24:
**[[3mji]] - BsPAH <br />
**[[3mji]] - BsPAH <br />
**[[2oqc]] - PAH – ''Bacillus subtilis''<br />
**[[2oqc]] - PAH – ''Bacillus subtilis''<br />
-
**[[4pel]], [[4pem]] - PAH α + β (mutant) subunits – ''Kluyvera cryocrescens''<br />
+
**[[4pel]], [[4pem]] - KcPAH α + β (mutant) subunits – ''Kluyvera cryocrescens''<br />
 +
**[[7reo]], [[7rep]] - KcPAH<br />
**[[3k3w]], [[3ml0]] - PAH precursor – ''Alcaligenes faecalis''<br />
**[[3k3w]], [[3ml0]] - PAH precursor – ''Alcaligenes faecalis''<br />
**[[6nvw]], [[6nvx]] - PAH G – ''Bacillus megaterium''<br />
**[[6nvw]], [[6nvx]] - PAH G – ''Bacillus megaterium''<br />

Current revision

E. coli penicillin acylase small α subunit (magenta) and large β subunit (deepskyblue) complex with penicillin and Ca+2 ion (green), 1fxv

Drag the structure with the mouse to rotate

3D structures of penicillin acylase

Updated on 05-December-2021

References

  1. Duggleby HJ, Tolley SP, Hill CP, Dodson EJ, Dodson G, Moody PC. Penicillin acylase has a single-amino-acid catalytic centre. Nature. 1995 Jan 19;373(6511):264-8. PMID:7816145 doi:http://dx.doi.org/10.1038/373264a0
  2. Volpato G, Rodrigues RC, Fernandez-Lafuente R. Use of enzymes in the production of semi-synthetic penicillins and cephalosporins: drawbacks and perspectives. Curr Med Chem. 2010;17(32):3855-73. PMID:20858215
  3. Alkema WB, Hensgens CM, Kroezinga EH, de Vries E, Floris R, van der Laan JM, Dijkstra BW, Janssen DB. Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies. Protein Eng. 2000 Dec;13(12):857-63. PMID:11239085

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Michal Harel, Alexander Berchansky

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