The stereochemistry of ketoreduction

被引:28
作者
Caffrey, P [1 ]
机构
[1] Univ Coll Dublin, Sch Biomol & Biomed Sci, Dublin 2, Ireland
[2] Univ Coll Dublin, Ctr Synth & Chem Biol, Dublin 2, Ireland
来源
CHEMISTRY & BIOLOGY | 2005年 / 12卷 / 10期
关键词
D O I
10.1016/j.chembiol.2005.10.002
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
In this issue of Chemistry & Biology, Leadlay and coworkers [1] report overproduction of a number of ketoreductase domains from modular polyketide synthases. These discrete enzymes allow the stereochemistry of polyketide ketoreduction to be studied in isolation.
引用
收藏
页码:1060 / 1062
页数:3
相关论文
共 14 条
[1]   Engineering of a minimal modular polyketide synthase, and targeted alteration of the stereospecificity of polyketide chain extension [J].
Bohm, I ;
Holzbaur, IE ;
Hanefeld, U ;
Cortes, J ;
Staunton, J ;
Leadlay, PF .
CHEMISTRY & BIOLOGY, 1998, 5 (08) :407-412
[2]   Conserved amino acid residues correlating with ketoreductase stereospecificity in modular polyketicle synthases [J].
Caffrey, P .
CHEMBIOCHEM, 2003, 4 (07) :654-657
[3]   Molecular basis of Celmer's rules: the role of two ketoreductase domains in the control of chirality by the erythromycin modular polyketide synthase [J].
Holzbaur, IE ;
Harris, RC ;
Bycroft, M ;
Cortes, J ;
Bisang, C ;
Staunton, J ;
Rudd, BAM ;
Leadlay, PF .
CHEMISTRY & BIOLOGY, 1999, 6 (04) :189-195
[4]   Molecular basis of Celmer's rules: role of the ketosynthase domain in epimerisation and demonstration that ketoreductase domains can have altered product specificity with unnatural substrates [J].
Holzbaur, IE ;
Ranganathan, A ;
Thomas, IP ;
Kearney, DJA ;
Reather, JA ;
Rudd, BAM ;
Staunton, J ;
Leadlay, PF .
CHEMISTRY & BIOLOGY, 2001, 8 (04) :329-340
[5]   Alcohol stereochemistry in polyketide backbones is controlled by the β-ketoreductase domains of modular polyketide synthases [J].
Kao, CM ;
McPherson, M ;
McDaniel, RN ;
Fu, H ;
Cane, DE ;
Khosla, C .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (10) :2478-2479
[6]   STEREOSPECIFIC ACYL TRANSFERS ON THE ERYTHROMYCIN-PRODUCING POLYKETIDE SYNTHASE [J].
MARSDEN, AFA ;
CAFFREY, P ;
APARICIO, JF ;
LOUGHRAN, MS ;
STAUNTON, J ;
LEADLAY, PF .
SCIENCE, 1994, 263 (5145) :378-380
[7]   Stereochemistry of catalysis by the ketoreductase activity in the first extension module of the erythromycin polyketide synthase [J].
Ostergaard, LH ;
Kellenberger, L ;
Cortés, J ;
Roddis, MP ;
Deacon, M ;
Staunton, J ;
Leadlay, PF .
BIOCHEMISTRY, 2002, 41 (08) :2719-2726
[8]   Type I polyketide biosynthesis in bacteria (Part B) [J].
Rawlings, BJ .
NATURAL PRODUCT REPORTS, 2001, 18 (03) :231-281
[9]   A model of structure and catalysis for ketoreductase domains in modular polyketide synthases [J].
Reid, R ;
Piagentini, M ;
Rodriguez, E ;
Ashley, G ;
Viswanathan, N ;
Carney, J ;
Santi, DV ;
Hutchinson, CR ;
McDaniel, R .
BIOCHEMISTRY, 2003, 42 (01) :72-79
[10]   Molecular basis of Celmer's rules: Stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases [J].
Siskos, AP ;
Baerga-Ortiz, A ;
Bali, S ;
Stein, V ;
Mamdani, H ;
Spiteller, D ;
Popovic, B ;
Spencer, JB ;
Staunton, J ;
Weissman, KJ ;
Leadlay, PF .
CHEMISTRY & BIOLOGY, 2005, 12 (10) :1145-1153