Regulation and structure of YahD, a copper-inducible / serine hydrolase of Lactococcus lactis IL1403

Martinez, Jacobo; Mancini, Stefano; Tauberger, Eva; Weise, Christoph; Saenger, Wolfram; Solioz, Marc (2011). Regulation and structure of YahD, a copper-inducible / serine hydrolase of Lactococcus lactis IL1403. FEMS microbiology letters, 314(1), pp. 57-66. Malden, Mass.: Blackwell Publishing Ltd 10.1111/j.1574-6968.2010.02144.x

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Lactococcus lactis IL1403 is a lactic acid bacterium that is used widely for food fermentation. Copper homeostasis in this organism chiefly involves copper secretion by the CopA copper ATPase. This enzyme is under the control of the CopR transcriptional regulator. CopR not only controls its own expression and that of CopA, but also that of an additional three operons and two monocistronic genes. One of the genes under the control of CopR, yahD, encodes an α/β-hydrolase. YahD expression was induced by copper and cadmium, but not by other metals or oxidative or nitrosative stress. The three-dimensional structure of YahD was determined by X-ray crystallography to a resolution of 1.88 Å. The protein was found to adopt an α/β-hydrolase fold with the characteristic Ser-His-Asp catalytic triad. Functional testing of YahD for a wide range of substrates for esterases, lipases, epoxide hydrolases, phospholipases, amidases and proteases was, however, unsuccessful. A copper-inducible serine hydrolase has not been described previously and YahD appears to be a new functional member of this enzyme family.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Gastro-intestinal, Liver and Lung Disorders (DMLL) > Clinic of Visceral Surgery and Medicine > Hepatology

UniBE Contributor:

Solioz, Marc

ISSN:

0378-1097

Publisher:

Blackwell Publishing Ltd

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:11

Last Modified:

23 Oct 2019 14:49

Publisher DOI:

10.1111/j.1574-6968.2010.02144.x

PubMed ID:

21059179

Web of Science ID:

000284963500008

BORIS DOI:

10.7892/boris.1739

URI:

https://boris.unibe.ch/id/eprint/1739 (FactScience: 203679)

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