کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8294246 | 1536751 | 2018 | 17 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural features and kinetic characterization of alanine racemase from Bacillus pseudofirmus OF4
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Alanine racemase (Alr) is a pyridoxal-5â²-phosphate-dependent (PLP) enzyme that catalyzes a reversible racemization between the enantiomers of alanine. d-Alanine is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan, and its inhibition is lethal to prokaryotes, which makes it an attractive target for designing antibacterial drugs. In this study, the molecular structure of alanine racemase from Bacillus pseudofirmus OF4 (DadXOF4) was determined by X-ray crystallography to a resolution of 1.8â¯Ã
. The comparison of DadXOF4 with alanine racemases from other bacteria demonstrated a conserved overall fold. Enzyme kinetics analysis showed that the conserved residues at the substrate entryway and the salt bridge at the dimer interface are critical for enzyme activity. These structural and biochemical findings provide a template for future structure-based drug-development efforts targeting alanine racemases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 497, Issue 1, 26 February 2018, Pages 139-145
Journal: Biochemical and Biophysical Research Communications - Volume 497, Issue 1, 26 February 2018, Pages 139-145
نویسندگان
Hui Dong, Tingting Hu, Guangzheng He, Deren Lu, Jianxun Qi, Yanshu Dou, Wei Long, Xin He, Jiansong Ju, Dan Su,