Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids

被引:139
作者
Altenbuchner, J
Siemann-Herzberg, M
Syldatk, C
机构
[1] Univ Stuttgart, Inst Ind Genet, D-70569 Stuttgart, Germany
[2] Univ Stuttgart, Inst Biochem Engn, D-70569 Stuttgart, Germany
关键词
D O I
10.1016/S0958-1669(01)00263-4
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
A cascade of hydantoinase, N-carbamoylase and hydantoinracemase can be used for the production of natural and unnatural chiral D- and L-amino acids from chemically synthesized hydantoin derivatives. Potentially, 100% conversion and 100% optically pure amino acids can be obtained at the same time if racemic substrates are used. Recent research activities concentrate on newly isolated or improved enzymes and include directed evolution techniques, structure elucidation, studies of fusion proteins and the use of specially designed whole cell biocatalysts.
引用
收藏
页码:559 / 563
页数:5
相关论文
共 25 条
[11]   Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases [J].
Nakai, T ;
Hasegawa, T ;
Yamashita, E ;
Yamamoto, M ;
Kumasaka, T ;
Ueki, T ;
Nanba, H ;
Ikenaka, Y ;
Takahashi, S ;
Sato, M ;
Tsukihara, T .
STRUCTURE, 2000, 8 (07) :729-737
[12]   Microbial enzymes: new industrial applications from traditional screening methods [J].
Ogawa, J ;
Shimizu, S .
TRENDS IN BIOTECHNOLOGY, 1999, 17 (01) :13-21
[13]   Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase [J].
Park, JH ;
Kim, GJ ;
Kim, HS .
BIOTECHNOLOGY PROGRESS, 2000, 16 (04) :564-570
[14]   Purification of recombinant hydantoinase and L-N-carbamoylase from Arthrobacter aurescens expressed in Escherichia coli:: comparison of wild-type and genetically modified proteins [J].
Pietzsch, M ;
Wiese, A ;
Ragnitz, K ;
Wilms, B ;
Altenbuchner, J ;
Mattes, R ;
Syldatk, C .
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES, 2000, 737 (1-2) :179-186
[15]   Optimization of the immobilization parameters and operational stability of immobilized hydantoinase and L-N-carbamoylase from Arthrobacter aurescens for the production of optically pure L-amino acids [J].
Ragnitz, K ;
Syldatk, C ;
Pietzsch, M .
ENZYME AND MICROBIAL TECHNOLOGY, 2001, 28 (7-8) :713-720
[16]   Two-step purification of D(-)-specific carbamoylase from Agrobacterium tumefaciens AM 10 [J].
Sareen, D ;
Sharma, R ;
Nandanwar, HS ;
Vohra, RM .
PROTEIN EXPRESSION AND PURIFICATION, 2001, 21 (01) :170-175
[17]   Identification, purification, and characterization of a thermophilic imidase from pig liver [J].
Su, TM ;
Yang, YS .
PROTEIN EXPRESSION AND PURIFICATION, 2000, 19 (02) :289-297
[18]  
Syldatk C., 1992, MICROBIAL ENZYMATIC
[19]  
SYLDATK C, 1995, HYDROLYSIS FORMATION, V1
[20]   Cloning and characterization of the Caenorhabditis elegans CeCRMP/DHP-1 and -2;: common ancestors of CRMP and dihydropyrimidinase? [J].
Takemoto, T ;
Sasaki, Y ;
Hamajima, N ;
Goshima, Y ;
Nonaka, M ;
Kimura, H .
GENE, 2000, 261 (02) :259-267