Penicillin acylase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
{{STRUCTURE_1fxv| PDB=1fxv | SIZE=400| SCENE= |right|CAPTION=''E. coli'' penicillin acylase small α subunit (grey) and large β subunit (green) complex with penicillin and Ca+2 ion (green), [[1fxv]] }} | {{STRUCTURE_1fxv| PDB=1fxv | SIZE=400| SCENE= |right|CAPTION=''E. coli'' penicillin acylase small α subunit (grey) and large β subunit (green) complex with penicillin and Ca+2 ion (green), [[1fxv]] }} | ||
== Function == | == 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. | + | '''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<ref>PMID:7816145</ref>. |
== Relevance == | == Relevance == | ||
PAH is used commercially for production of semi-synthetic penicillins. | PAH is used commercially for production of semi-synthetic penicillins. | ||
| + | |||
| + | == Structural highlights == | ||
| + | |||
| + | PAH contains a β-lactam binding site between its 2 subunits<ref>PMID:11239085</ref>. | ||
==3D structures of penicillin acylase== | ==3D structures of penicillin acylase== | ||
| Line 32: | Line 36: | ||
**[[2z71]] - BsPAH (mutant) + penicillin | **[[2z71]] - BsPAH (mutant) + penicillin | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:29, 19 June 2016
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.
Structural highlights
PAH contains a β-lactam binding site between its 2 subunits[2].
3D structures of penicillin acylase
Updated on 19-June-2016
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
- ↑ 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
