Penicillin acylase

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== Relevance ==
== Relevance ==
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PAH is used commercially for production of semi-synthetic penicillins.
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PAH is used commercially for production of semi-synthetic penicillins<ref>PMID:20858215</ref>.
== Structural highlights ==
== Structural highlights ==

Revision as of 09:31, 19 June 2016

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Contents

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 β-lactam binding site between its 2 subunits[3].

3D structures of penicillin acylase

Updated on 19-June-2016

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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