Effect of cell membrane of Agrobacterium radiobacter on enhancing D-amino acids production from racemic hydantoins

Enzyme and Microbial Technology

Volumn 28, Issue 9-10, 2001, Pages 806-814

  Lee, Cheng Kang ^a   Lee, Zong Shang ^a   Yang, Pei Fen ^a  

^a NATIONAL TAIWAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CELLS; DERIVATIVES; ENZYMES; MECHANICAL PERMEABILITY;

INTRACELLULAR ENZYMES;

AMINO ACIDS;

AMIDASE; CELL ENZYME; DEXTRO AMIDOHYDROLASE; DEXTRO AMINO ACID; DEXTRO HYDANTOINASE; DIHYDROPYRIMIDINASE; HYDANTOIN DERIVATIVE; RACEMIC HYDANTOIN DERIVATIVE; TOLUENE; UNCLASSIFIED DRUG;

ARTICLE; CELL ACTIVITY; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; ENZYME ACTIVITY; MATHEMATICAL MODEL; NONHUMAN; RHIZOBIUM RADIOBACTER;

AGROBACTERIUM TUMEFACIENS; RADIOBACTER;

EID: 0035822002     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(01)00334-9     Document Type: Article

References (10)

1. Microbial enzymes as catalysts for synthesis of biologically useful compounds
2. Hydrolysis and formation of hydantoins
3. Microbial transformation of racemic hydantoins to D-amino acids
4. D-p-Hydroxyphenylglycine production from D, L-5-p-hydroxyphenylhydantoin by Agrobacterium sp.
5. Modeling and control of the biocatalytic conversion of hydantoins to D-amino acids
6. Optimization of the enzymatic synthesis of D-p-hydroxyphenylglycine from D, L-5-substituted hydantoin using D-hydantoinase and N-carbamoylase
7. Enzymatic synthesis and subsequent racemization rates determination of optically active D-5-phenylhydantoin and D-5-hydroxyphenylhydantoin
8. Production of D-p-hydroxyphenylglycine by N-carbamoyl-D-amino acid amidohydrolase-overproducing Escherichia coli strains
9. Cloning and over-expression of thermostable D-hydantoinase from thermophilie in E. coli and its application to the synthesis of optically active D-amino acids
10. Identification, sequencing, and mutagenesis of the gene for a D-carbamoylase from Agrobacterium radiobacter