کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9121465 | 1159187 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular cloning and functional analysis of (R)-3-hydroxyacyl-acyl carrier protein:coenzyme A transacylase from Pseudomonas mendocina LZ
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
An inactive (R)-3-hydroxyacyl-acyl carrier protein:coenzyme A transacylase (PhaGPm) was cloned from a newly isolated Proteobacteria Pseudomonas mendocina LZ. It is the first characterized native inactive PhaG protein. Sequence analysis indicated that there were only two sites where the amino acid sequence differed between this inactive protein and the functional PhaGPp from P. putida. The differences were located at position 78 and in the region 109-113 in the amino acid sequence. Mutagenesis was carried out to investigate these two sites. A recombinant strain harboring a S78C PhaGPp mutant accumulated polyhydroxyalkanoates (PHA) at 11.9% of the cellular dry weight, as compared to the 21.6% PHA produced by the recombinant harboring the wild-type PhaGPp. On the other hand, the changes in the amino acid region 109-113 of PhaGPp to its corresponding region of PhaGPm resulted in negligible PHA accumulation. This demonstrated that region 109-113 in PhaG is relatively important for transacylase activity, while position 78 just plays a supporting role for the enzyme. Furthermore, 3-D structural models of PhaGPp and PhaGPm developed by computational prediction revealed that the variation in amino acids at 109-113 leads to the destruction of the PhaG catalytic center, resulting in the loss of enzyme activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEMS Microbiology Letters - Volume 252, Issue 2, 15 November 2005, Pages 299-307
Journal: FEMS Microbiology Letters - Volume 252, Issue 2, 15 November 2005, Pages 299-307
نویسندگان
Leo Zhong Zheng, Zhi Li, Hong-Lei Tian, Ming Li, Guo-Qiang Chen,