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Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica
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Mustakhimov, Ildar I., Rozova, Olga N., Reshetnikov, Alexander S., Khmelenina, V. N. (Valentina Nikolaevna), Murrell, J. C. (J. Colin) and Trotsenko, Yuri A.. (2008) Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica. FEMS Microbiology Letters, Vol.283 (No.1). pp. 91-96. ISSN 0378-1097
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Official URL: http://dx.doi.org/10.1111/j.1574-6968.2008.01156.x
Abstract
Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to gamma-N-acetyl-alpha,gamma-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 33146(T) and Methylophaga alcalica ATCC 35842(T). 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 degrees C), K-m for diaminobutyrate (370 or 375 mu M) 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.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QR Microbiology |
| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) |
| Library of Congress Subject Headings (LCSH): | Enzymes, Biosynthesis, Proteins -- Purification, Halophilic microorganisms, Methylotrophic bacteria, Acetyltransferases |
| Journal or Publication Title: | FEMS Microbiology Letters |
| Publisher: | Wiley-Blackwell Publishing Ltd. |
| ISSN: | 0378-1097 |
| Date: | June 2008 |
| Volume: | Vol.283 |
| Number: | No.1 |
| Number of Pages: | 6 |
| Page Range: | pp. 91-96 |
| Identification Number: | 10.1111/j.1574-6968.2008.01156.x |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| URI: | http://wrap.warwick.ac.uk/id/eprint/30158 |
Data sourced from Thomson Reuters' Web of Knowledge
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