Open AccessRegulation and structure of YahD, a copper‐inducible α/β serine hydrolase of Lactococcus lactis IL1403
Author(s) -
Martinez Jacobo,
Mancini Stefano,
Tauberger Eva,
Weise Christoph,
Saenger Wolfram,
Solioz Marc
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2010.02144.x
Subject(s) - lactococcus lactis , serine hydrolase , hydrolase , catalytic triad , biochemistry , epoxide hydrolase , operon , serine , chemistry , enzyme , biology , proteases , bacteria , gene , lactic acid , mutant , genetics , microsome
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.