Literature summary for 3.5.1.87 extracted from

Hsu, S.; Lo, H.; Lin, W.; Chen, I.; Kao, C.; Hsu, W.
Stereoselective synthesis of L-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase (2007), Process Biochem., 42, 856-862.

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Application

Application	Comment	Organism
synthesis	to develop a recombinant Escherichia coli whole cell system for the conversion of racemic N-carbamoyl-L-homophenylalanine to L-homophenylalanine, naaar gene from Deinococcus radiodurans and L-N-carbamoylase gene from Bacillus kaustophilus BCRC11223 are cloned and coexpressed in Escherichia coli cells. Recombinant cells treated with 0.5% toluene at 30°C for 30 min exhibit enhanced N-acylamino acid racemase and L-N-carbamoylase activities, which are about 20fold and 60fold, respectively, higher than those of untreated cells. Using toluene-permeabilized recombinant Escherichia coli cells, a maximal productivity of 7.5 mmol L-homophenylalanine/l h with more than 99% yield could be obtained from 150 mmol racemic N-carbamoyl-D-homophenylalanine. Permeabilized cells show considerable stability in the bioconversion process using 10 mmol racemic N-carbamoyl-D-homophenylalanine as substrate, no significantly decrease in conversion yield for L-homophenylalanine is found in the eight cycles	Geobacillus kaustophilus

Cloned(Commentary)

Cloned (Comment)	Organism
-	Geobacillus kaustophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus kaustophilus	-	BCRC11223	-
Geobacillus kaustophilus BCRC11223	-	BCRC11223	-

Synonyms

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

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Release 2023.1 (January 2023)