Sirtuins caught in the act

被引：11

作者：

Smith, Brian C. ^{[1
]}

Denu, John M.

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Univ Wisconsin, Dept Biomol Chem, Madison, WI 53706 USA

来源：

STRUCTURE | 2006年 / 14卷 / 08期

关键词：

D O I：

10.1016/j.str.2006.07.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Sirtuins catalyze the NAD(+)-dependent protein deacetylation of lysine residues. In this issue of Structure, Hoff et al. (2006) report the structure of a sirtuin homolog with both substrates bound, providing new insight into the catalytic mechanism.

引用

页码：1207 / 1208

页数：2

共 6 条

[1]

Structural basis for the mechanism and regulation of Sir2 enzymes [J].

Avalos, JL ;

Boeke, JD ;

Wolberger, C .

MOLECULAR CELL, 2004, 13 (05) :639-648

[2]

The Sir2 family of protein deacetylases [J].

Blander, G ;

Guarente, L .

ANNUAL REVIEW OF BIOCHEMISTRY, 2004, 73 :417-435

[3]

Vitamin B3 and sirtuin function [J].

Denu, JM .

TRENDS IN BIOCHEMICAL SCIENCES, 2005, 30 (09) :479-483

[4]

Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases [J].

Jackson, MD ;

Schmidt, MT ;

Oppenheimer, NJ ;

Denu, JM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (51) :50985-50998

[5]

The silencing protein SIR2 and its homologs are MAD-dependent protein deacetylases [J].

Landry, J ;

Sutton, A ;

Tafrov, ST ;

Heller, RC ;

Stebbins, J ;

Pillus, L ;

Sternglanz, R .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (11) :5807-5811

[6]

Sir2 protein deacetylases: Evidence for chemical intermediates and functions of a conserved histidine [J].

Smith, BC ;

Denu, JM .

BIOCHEMISTRY, 2006, 45 (01) :272-282

← 1 →