NDLI: Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Content Provider	Springer Nature Link
Author	Engel, U. Syldatk, C. Rudat, J.
Copyright Year	2011
Abstract	In this study, we investigated the possibility of using a modified hydantoinase process for the production of optically pure β-amino acids. Two aryl-substituted dihydropyrimidines d,l-6-phenyl-5,6-dihydrouracil (PheDU) and para-chloro-d,l-6-phenyl-5,6-dihydrouracil (pClPheDU) were synthesized. Hydrolysis of these novel substrates to the corresponding N-carbamoyl-β-amino acids by three recombinant d-hydantoinases and several bacterial strains was tested. All applied recombinant d-hydantoinases and eight bacterial isolates catalyzed the conversion of PheDU to N-carbamoyl-β-phenylalanine (NCβPhe). Some of these biocatalysts showed an enantioselectivity for either the d- or the l-PheDU enantiomer. The second dihydropyrimidinase substrate pClPheDU was hydrolyzed by all three recombinant d-hydantoinases and six of the wild-type strains. To our knowledge, this is the first dihydropyrimidinase activity reported with this aryl-substituted dihydropyrimidine. For selected biocatalysts, hydantoinase activity towards aryl-substituted hydantoins was demonstrated as well. However, none of the bacterial strains tested so far exhibited any carbamoylase activity towards NCβPhe.
Starting Page	1221
Ending Page	1231
Page Count	11
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	94
Issue Number	5
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-11-27
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Beta-amino acid Hydantoinase Dihydropyrimidinase Carbamoylase Microbiology Biotechnology Microbial Genetics and Genomics
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences.

Carbamoylases: characteristics and applications in biotechnological processes

Imidase catalyzing desymmetric imide hydrolysis forming optically active 3-substituted glutaric acid monoamides for the synthesis of gamma-aminobutyric acid (GABA) analogs

Enzymatic dynamic kinetic resolution of racemic N-formyl- and N-carbamoyl-amino acids using immobilized l-N-carbamoylase and N-succinyl-amino acid racemase

Enzymatic production of l-amino acids from the corresponding dl-5-substituted hydantoins by Bacillus fordii MH602

Enhancing the catalytic potential of nitrilase from Pseudomonas putida for stereoselective nitrile hydrolysis

Bacterial β-peptidyl aminopeptidases: on the hydrolytic degradation of β-peptides

Overproduction of d-hydantoinase and carbamoylase in a soluble form in Escherichia coli

Bacterial defluorination of 4-fluoroglutamic acid

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Similar Documents

Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences.

Carbamoylases: characteristics and applications in biotechnological processes

Imidase catalyzing desymmetric imide hydrolysis forming optically active 3-substituted glutaric acid monoamides for the synthesis of gamma-aminobutyric acid (GABA) analogs

Enzymatic dynamic kinetic resolution of racemic N-formyl- and N-carbamoyl-amino acids using immobilized l-N-carbamoylase and N-succinyl-amino acid racemase

Enzymatic production of l-amino acids from the corresponding dl-5-substituted hydantoins by Bacillus fordii MH602

Enhancing the catalytic potential of nitrilase from Pseudomonas putida for stereoselective nitrile hydrolysis

Bacterial β-peptidyl aminopeptidases: on the hydrolytic degradation of β-peptides

Overproduction of d-hydantoinase and carbamoylase in a soluble form in Escherichia coli

Bacterial defluorination of 4-fluoroglutamic acid

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases