Penicillin acylase
From Proteopedia
(Difference between revisions)
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**[[4pel]], [[4pem]] - PAH α + β (mutant) subunits – ''Kluyvera cryocrescens''<br /> | **[[4pel]], [[4pem]] - PAH α + β (mutant) subunits – ''Kluyvera cryocrescens''<br /> | ||
**[[3k3w]], [[3ml0]] - PAH precursor – ''Alcaligenes faecalis''<br /> | **[[3k3w]], [[3ml0]] - PAH precursor – ''Alcaligenes faecalis''<br /> | ||
| + | **[[6nvw]], [[6nvx]] - PAH G – ''Bacillus megaterium''<br /> | ||
| + | **[[6nvy]] - PAH G – ''Bacillus thermotolerans''<br /> | ||
*Penicillin acylase complex | *Penicillin acylase complex | ||
Revision as of 10:23, 13 November 2019
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3D structures of penicillin acylase
Updated on 13-November-2019
References
- ↑ 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
- ↑ 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
- ↑ 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
