کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10872019 | 1074095 | 2009 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mechanism of arginine regulation of acetylglutamate synthase, the first enzyme of arginine synthesis
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کلمات کلیدی
NAGNAGSGcn5-related N-acetyltransferaseN-acetyl-l-glutamateN-acetyl-l-glutamate kinaseaAKNAGKamino acid kinase - آمینو اسید کینازGlutamate binding - اتصال گلوتاماتArginine biosynthesis - بیوسنتز آرژینینPseudomonas aeruginosa - سودوموناس آئروژینوزاFeed-back inhibition - مهار خوراکNeisseria gonorrhoeae - نایسریا گونوره آwild-type - نوع وحشیGNAT - گنات
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
N-acetyl-l-glutamate synthase (NAGS), the first enzyme of arginine biosynthesis in bacteria/plants and an essential urea cycle activator in animals, is, respectively, arginine-inhibited and activated. Arginine binds to the hexameric ring-forming amino acid kinase (AAK) domain of NAGS. We show that arginine inhibits Pseudomonas aeruginosa NAGS by altering the functions of the distant, substrate binding/catalytic GCN5-related N-acetyltransferase (GNAT) domain, increasing KmGlu, decreasing Vmax and triggering substrate inhibition by AcCoA. These effects involve centrally the interdomain linker, since we show that linker elongation or two-residue linker shortening hampers and mimics, respectively, arginine inhibition. We propose a regulatory mechanism in which arginine triggers the expansion of the hexameric NAGS ring, altering AAK-GNAT domain interactions, and the modulation by these interactions of GNAT domain functions, explaining arginine regulation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 583, Issue 1, 5 January 2009, Pages 202-206
Journal: FEBS Letters - Volume 583, Issue 1, 5 January 2009, Pages 202-206
نویسندگان
Enea Sancho-Vaello, MarÃa L. Fernández-Murga, Vicente Rubio,