Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M311194200
DC FieldValue
dc.titleSpecificity and Enzyme Kinetics of the Quorum-quenching N-Acyl Homoserine Lactone Lactonase (AHL-lactonase)
dc.contributor.authorWang, L.-H.
dc.contributor.authorWeng, L.-X.
dc.contributor.authorDong, Y.-H.
dc.contributor.authorZhang, L.-H.
dc.date.accessioned2014-10-27T08:40:09Z
dc.date.available2014-10-27T08:40:09Z
dc.date.issued2004-04-02
dc.identifier.citationWang, L.-H., Weng, L.-X., Dong, Y.-H., Zhang, L.-H. (2004-04-02). Specificity and Enzyme Kinetics of the Quorum-quenching N-Acyl Homoserine Lactone Lactonase (AHL-lactonase). Journal of Biological Chemistry 279 (14) : 13645-13651. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M311194200
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101711
dc.description.abstractN-Acyl homoserine lactone (AHL) quorum-sensing signals are the vital elements of bacterial quorum-sensing systems, which regulate diverse biological functions, including virulence. The AHL-lactonase, a quorum-quenching enzyme encoded by aiiA from Bacillus sp., inactivates AHLs by hydrolyzing the lactone bond to produce corresponding N-acyl homoserines. To characterize the enzyme, the recombinant AHL-lactonase and its four variants were purified. Kinetic and substrate specificity analysis showed that AHL-lactonase had no or little residue activity to non-acyl lactones and noncyclic esters, but displayed strong enzyme activity toward all tested AHLs, varying in length and nature of the substitution at the C3 position of the acyl chain. The data also indicate that the amide group and the ketone at the C1 position of the acyl chain of AHLs could be important structural features in enzyme-substrate interaction. Surprisingly, although carrying a 104HX-HXDH109 short sequence identical to the zinc-binding motif of several groups of metallohydrolytic enzymes, AHL-lactonase does not contain or require zinc or other metal ions for enzyme activity. Except for the amino acid residue His-104, which was shown previously to not be required for catalysis, kinetic study and conformational analysis using circular dichroism spectrometry showed that substitution of the other key residues in the motif (His-106, Asp-108, and His-109), as well as His-169 with serine, respectively, caused conformational changes and significant loss of enzyme activity. We conclude that AHL-lactonase is a highly specific enzyme and that the 106HXDH109∼ H169 of AHL-lactonase represents a novel catalytic motif, which does not rely on zinc or other metal ions for activity.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M311194200
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1074/jbc.M311194200
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume279
dc.description.issue14
dc.description.page13645-13651
dc.description.codenJBCHA
dc.identifier.isiut000220478500046
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.