Academic Journal

Functional Analysis of All Aminotransferase Proteins Inferred from the Genome Sequence of Corynebacterium glutamicum

التفاصيل البيبلوغرافية
العنوان: Functional Analysis of All Aminotransferase Proteins Inferred from the Genome Sequence of Corynebacterium glutamicum
المؤلفون: Marienhagen, Jan, Kennerknecht, Nicole, Sahm, Hermann, Eggeling, Lothar
المصدر: Journal of Bacteriology ; volume 187, issue 22, page 7639-7646 ; ISSN 0021-9193 1098-5530
بيانات النشر: American Society for Microbiology
سنة النشر: 2005
الوصف: Twenty putative aminotransferase (AT) proteins of Corynebacterium glutamicum , or rather pyridoxal-5′-phosphate (PLP)-dependent enzymes, were isolated and assayed among others with l -glutamate, l -aspartate, and l -alanine as amino donors and a number of 2-oxo-acids as amino acceptors. One outstanding AT identified is AlaT, which has a broad amino donor specificity utilizing (in the order of preference) l -glutamate > 2-aminobutyrate > l -aspartate with pyruvate as acceptor. Another AT is AvtA, which utilizes l -alanine to aminate 2-oxo-isovalerate, the l -valine precursor, and 2-oxo-butyrate. A second AT active with the l -valine precursor and that of the other two branched-chain amino acids, too, is IlvE, and both enzyme activities overlap partially in vivo, as demonstrated by the analysis of deletion mutants. Also identified was AroT, the aromatic AT, and this and IlvE were shown to have comparable activities with phenylpyruvate, thus demonstrating the relevance of both ATs for l -phenylalanine synthesis. We also assessed the activity of two PLP-containing cysteine desulfurases, supplying a persulfide intermediate. One of them is SufS, which assists in the sulfur transfer pathway for the Fe-S cluster assembly. Together with the identification of further ATs and the additional analysis of deletion mutants, this results in an overview of the ATs within an organism that may not have been achieved thus far.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1128/jb.187.22.7639-7646.2005
DOI: 10.1128/JB.187.22.7639-7646.2005
الاتاحة: http://dx.doi.org/10.1128/jb.187.22.7639-7646.2005
https://journals.asm.org/doi/pdf/10.1128/JB.187.22.7639-7646.2005
Rights: https://journals.asm.org/non-commercial-tdm-license
رقم الانضمام: edsbas.BA056207
قاعدة البيانات: BASE
الوصف
DOI:10.1128/jb.187.22.7639-7646.2005