Penicillin acylase

From Proteopedia

Revision as of 08:07, 30 August 2017

spinqualitylabelsall models E. coli penicillin acylase small α subunit (magenta) and large β subunit (deepskyblue) complex with penicillin and Ca+2 ion (green), 1fxv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Penicillin acylase (PAH) catalyzes the conversion of penicillin to 6-amino-penicillanate and phenylacetate (PA). PAH contains 2 non-identical subunits. The larger β subunit contains a phenylmethylsulfonyl residue which is required for enzymatic activity. PAH participates in penicillin and cephalosporin biosynthesis[1]. Relevance PAH is used commercially for production of semi-synthetic penicillins[2]. Structural highlights PAH contains a [3]. is also located between its 2 subunits.

3D structures of penicillin acylase

Updated on 30-August-2017

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