Literature summary for 3.5.1.87 extracted from

Kao, C.H.; Lo, H.H.; Hsu, S.K.; Hsu, W.H.
A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and L-N-carbamoylase activities as biocatalyst for the production of L-homophenylalanine (2008), J. Biotechnol., 134, 231-239.

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Application

Application	Comment	Organism
synthesis	production of a cell biocatalyst for the production of L-homophenylalanine from D,L-homophenylalanylhydantoin by coexpression of the pydB gene and a thermostable L-N-carbamoylase gene from Bacillus kaustophilus CCRC11223 in Escherichia coli JM109. The expression levels of dihydropyrimidinase and l-N-carbamoylase in the recombinant Escherichia coli cells are estimated to be about 20% of the respective total soluble proteins. When 1% (w/v) isopropyl-beta-D-thiogalactopyranoside-induced cells are used as biocatalysts, a conversion yield of 49% for D,L-homophenylalanylhydantoin with more than 99% enantiomeric excess can be reached in 16 h at pH 7.0 from 10 mM D,L-homophenylalanylhydantoin. The cells can be reused for at least eight cycles at a conversion yield of more than 43%. Coexpression of pydB and lnc in Escherichia coli might be a potential biocatalyst for production of L-homophenylalanylhydantoin	Geobacillus kaustophilus

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Geobacillus kaustophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus kaustophilus	-	CCRC11223	-
Geobacillus kaustophilus CCRC 11223	-	CCRC11223	-

Synonyms

Synonyms	Comment	Organism
L-N-carbamoylase	-	Geobacillus kaustophilus
Lnc	-	Geobacillus kaustophilus

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Release 2023.1 (January 2023)