Threonine Aldolases

被引:46
作者
Franz, Sarah E. [1 ]
Stewart, Jon D. [1 ]
机构
[1] Univ Florida, Dept Chem, Gainesville, FL 32611 USA
来源
ADVANCES IN APPLIED MICROBIOLOGY, VOL 88 | 2014年 / 88卷
关键词
ALPHA-AMINO ACIDS; PLP-DEPENDENT ALDOLASE; ORGANIC-SYNTHESIS; ESCHERICHIA-COLI; ENZYMATIC-SYNTHESIS; KEY INTERMEDIATE; GENE CLONING; STEREOSELECTIVITY; MECHANISM; RACEMASE;
D O I
10.1016/B978-0-12-800260-5.00003-6
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Threonine aldolases catalyze the pyridoxal phosphate-dependent condensation between small amino acids (principally glycine) and aldehydes such as acetaldehyde. Carbon carbon bond formation involves forming two adjacent chiral centers. As a rule, threonine aldolases are very stereoselective for a-carbon configuration but show modest selectivity at the beta-carbon. On the other hand, these enzymes accept a wide variety of synthetically useful acceptor aldehydes, making them important additions to the synthetic toolkit. This review briefly summarizes the reaction mechanism and then lists all published synthetic reactions by threonine aldolases as of early 2014. The current state of the art in crystallographic and protein engineering studies of these enzymes is also presented.
引用
收藏
页码:57 / 101
页数:45
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