Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica

II Mustakhimov, ON Rozova, AS Reshetnikov, VN Khmelenina, JC Murrell, YA Trotsenko

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Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.
Original languageEnglish
Pages (from-to)91-96
Number of pages6
JournalFEMS Microbiology Letters
Issue number1
Publication statusPublished - 2008

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