Evolution of vitamin B2 biosynthesis: eubacterial RibG and fungal Rib2 deaminases

doi:10.1107/S0907444912044903

中山醫學大學機構典藏 CSMUIR > 醫學科技學院 > 醫學檢驗暨生物技術學系暨碩士班 > 期刊論文 > Item 310902500/15965

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题名:	Evolution of vitamin B2 biosynthesis: eubacterial RibG and fungal Rib2 deaminases
作者:	SC, Chen CY, Shen TM, Yen HC, Yu TH, Chang WL, Lai SH, Liaw
贡献者:	中山醫學大學
关键词:	Rib2;RibG;amino-binding hole;mutational analysis;riboflavin biosynthesis
日期:	2013
上传时间:	2016-09-06T08:43:53Z (UTC)
ISSN:	0907-4449
摘要:	Eubacterial RibG and yeast Rib2 possess a deaminase domain for pyrimidine deamination in the second and third steps, respectively, of riboflavin biosynthesis. These enzymes are specific for ribose and ribitol, respectively. Here, the crystal structure of Bacillus subtilis RibG in complex with a deaminase product is reported at 2.56 Å resolution. Two loops move towards the product on substrate binding, resulting in interactions with the ribosyl and phosphate groups and significant conformational changes. The product carbonyl moiety is bent out of the pyrimidine ring to coordinate to the catalytic zinc ion. Such distortions in the bound substrate and product may play an essential role in enzyme catalysis. The yeast Rib2 structure was modelled and a mutational analysis was carried out in order to understand the mechanism of substrate recognition in these two enzymes. Detailed structural comparisons revealed that the two consecutive carbonyl backbones that occur prior to the PCXXC signature constitute a binding hole for the target amino group of the substrate. This amino-binding hole is essential in B. subtilis RibG and is also conserved in the RNA/DNA-editing deaminases.
URI:	http://dx.doi.org/10.1107/S0907444912044903 https://ir.csmu.edu.tw:8080/ir/handle/310902500/15965
關聯:	Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):227-36.
显示于类别:	[醫學檢驗暨生物技術學系暨碩士班] 期刊論文

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