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1ai6

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Revision as of 10:41, 10 September 2015

PENICILLIN ACYLASE WITH P-HYDROXYPHENYLACETIC ACID

Structural highlights

1ai6 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Penicillin amidase, with EC number 3.5.1.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1. 11) catalyses the cleavage of the amide bond in the benzylpenicillin (penicillin G) side-chain to produce phenylacetic acid and 6-aminopenicillanic acid (6-APA). The enzyme is of great pharmaceutical importance, as the product 6-APA is the starting point for the synthesis of many semi-synthetic penicillin antibiotics. Studies have shown that the enzyme is specific for hydrolysis of phenylacetamide derivatives, but is more tolerant of features in the rest of the substrate. It is this property that has led to many other applications for the enzyme, and greater knowledge of the enzyme's structure and specificity could facilitate engineering of the enzyme, enhancing its potential for chemical and industrial applications. An extensive study of the binding of a series of phenylacetic acid derivatives has been carried out. A measure of the relative degree of inhibition of the enzyme by each of the compounds has been obtained using a competitive inhibition assay, and the structures of a number of these complexes have been determined by X-ray crystallography. The structures reveal a clear rationale for the observed kinetic results, but show also that some of the ligands cause a conformational change within the binding pocket. This change can generally be understood in terms of the size and orientation of the ligand within the active site.The results reveal that ligand binding in penicillin acylase is facilitated by certain amino acid residues that can adopt two distinct, energetically favourable positions in order to accommodate a variety of compounds within the active site. The structures of these complexes provide evidence for conformational changes in the substrate-binding region that may act as a switch in the mechanism of autocatalytic processing of this enzyme.

Ligand-induced conformational change in penicillin acylase.,Done SH, Brannigan JA, Moody PC, Hubbard RE J Mol Biol. 1998 Nov 27;284(2):463-75. PMID:9813130^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Done SH, Brannigan JA, Moody PC, Hubbard RE. Ligand-induced conformational change in penicillin acylase. J Mol Biol. 1998 Nov 27;284(2):463-75. PMID:9813130 doi:10.1006/jmbi.1998.2180

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ai6"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4HP:4-HYDROXYPHENYLACETATE'>4HP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ai6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai6 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai6 OCA], [http://pdbe.org/1ai6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ai6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai6 PDBsum]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ai6" style="background-color:#fffaf0;"></div>
 ==See Also==

1ai6

From Proteopedia

Revision as of 10:41, 10 September 2015

PENICILLIN ACYLASE WITH P-HYDROXYPHENYLACETIC ACID

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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