Evolution of NAD biosynthetic enzymes

被引：11

作者：

Brenner, C ^{[1
]}

机构：

[1] Dartmouth Coll Sch Med, Dept Genet, Lebanon, NH 03756 USA

来源：

STRUCTURE | 2005年 / 13卷 / 09期

关键词：

D O I：

10.1016/j.str.2005.08.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two research groups have solved crystal structures of nicotinic acid phosphoribosyltransferase (PRTase) and made the argument that PRTases in three distinct pathways of nicotinamide adenine dinucleotide (NAD) biosynthesis evolved from a common ancestor (Shin et al., 2005; Chappie et al., 2005).

引用

页码：1239 / 1240

页数：2

共 11 条

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