NDLI: Enzymatic Synthesis of High-Molecular-Mass Poly-γ-Glutamate and Regulation of Its Stereochemistry

Content Provider	PubMed Central
Author	Makoto, Ashiuchi Shimanouchi, Kazuya Nakamura, Hisaaki Kamei, Tohru Soda, Kenji Park, Chung Sung, Moon-hee Misono, Haruo
Copyright Year	2004
Abstract	For the first time, we succeeded in synthesizing in vitro poly-γ-glutamate (PGA) with high molecular masses (>1,000 kDa) by the use of enzyme-associated cell membranes from Bacillus subtilis subsp. chungkookjang. The activity for PGA synthesis, however, was readily lost in the presence of critical concentrations of detergents tested in micelles. The optimum pH for the reaction was found to be ∼7.0. We examined the effects of some divalent cations on PGA synthesis and found that Mg2+ was essential in catalysis and that Zn2+ additionally boosted the activity. In contrast, Fe2+ and Ca2+ acted as inhibitors. Mn2+ did not apparently influence the in vitro formation of PGA. dl-Glutamate (d isomer content, 60 to 80%) apparently served as the best substrate; d-Glutamate was preferable to the l isomer as a substrate. When d- and l-glutamate were used for the reaction, the elongated chains of PGAs were composed of the d- and l-isomers, respectively. Our results suggest that the stereochemical properties of enzymatically synthesized PGAs substantially depend on the stereochemistry (dl ratio) of glutamate as the substrate. Furthermore, genetic analysis indicated that all the pgsB, -C, and -A gene products, which are responsible for PGA production by B. subtilis cells, were also indispensable for enzymatic PGA synthesis.
Related Links	http://dx.doi.org/10.1128/AEM.70.7.4249-4255.2004
Starting Page	4249
File Format	PDF
ISSN	10985336
e-ISSN	10985336
Journal	Applied and Environmental Microbiology
Issue Number	7
Volume Number	70
Language	English
Publisher	American Society for Microbiology
Publisher Date	2004-07-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Ecology Food Science 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

Characterization of Poly-γ-Glutamate Hydrolase Encoded by a Bacteriophage Genome: Possible Role in Phage Infection of Bacillus subtilis Encapsulated with Poly-γ-Glutamate

Use of Bacterial γ-Glutamyltranspeptidase for Enzymatic Synthesis of γ-d-Glutamyl Compounds

Mutations Suppressing the Loss of DegQ Function in Bacillus subtilis (natto) Poly-γ-Glutamate Synthesis ▿ †

Calcium regulates glutamate dehydrogenase and poly-γ-glutamic acid synthesis in Bacillus natto

Regulation of Polyglutamic Acid Synthesis by Glutamate in Bacillus licheniformis and Bacillus subtilis

Expression of glr gene encoding glutamate racemase in Bacillus licheniformis WX-02 and its regulatory effects on synthesis of poly-γ-glutamic acid

Enzymatic Synthesis of Novel Phloretin Glucosides

Moonlighting Role of a Poly-γ-Glutamate Synthetase Component from Bacillus subtilis: Insight into Novel Extrachromosomal DNA Maintenance ▿ †

High-Temperature Enzymatic Breakdown of Cellulose▿ †

Enzymatic Synthesis of High-Molecular-Mass Poly-γ-Glutamate and Regulation of Its Stereochemistry

Similar Documents

Characterization of Poly-γ-Glutamate Hydrolase Encoded by a Bacteriophage Genome: Possible Role in Phage Infection of Bacillus subtilis Encapsulated with Poly-γ-Glutamate

Use of Bacterial γ-Glutamyltranspeptidase for Enzymatic Synthesis of γ-d-Glutamyl Compounds

Mutations Suppressing the Loss of DegQ Function in Bacillus subtilis (natto) Poly-γ-Glutamate Synthesis ▿ †

Calcium regulates glutamate dehydrogenase and poly-γ-glutamic acid synthesis in Bacillus natto

Regulation of Polyglutamic Acid Synthesis by Glutamate in Bacillus licheniformis and Bacillus subtilis

Expression of glr gene encoding glutamate racemase in Bacillus licheniformis WX-02 and its regulatory effects on synthesis of poly-γ-glutamic acid

Enzymatic Synthesis of Novel Phloretin Glucosides

Moonlighting Role of a Poly-γ-Glutamate Synthetase Component from Bacillus subtilis: Insight into Novel Extrachromosomal DNA Maintenance ▿ †

High-Temperature Enzymatic Breakdown of Cellulose▿ †

Enzymatic Synthesis of High-Molecular-Mass Poly-γ-Glutamate and Regulation of Its Stereochemistry