Structure of the Hydrolyzed Product (F-2) Released from γ-Polyglutamic Acid by γ-Glutamyl Hydrolase YwtD of Bacillus subtilis
スポンサーリンク
概要
- 論文の詳細を見る
The structure of the hydrolyzed product (F-2) with a molecular mass of about 2 kDa released from γ-polyglutamic acid by the γ-glutamyl hydrolase YwtD of Bacillus subtilis was analyzed. The results showed that F-2 is an optically heterogeneous polymer consisting of D- and L-glutamic acid in an 80:20 ratio with D-glutamic acid on both the N- and C-terminal sides, suggesting that YwtD is an enzyme that cleaves the γ-glutamyl bond between D- and D-glutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region.
- 社団法人 日本農芸化学会の論文
- 2007-09-23
著者
-
Tanimoto Hiroyuki
Processed Food Development And Technology Center Food Products Company Ajinomoto Co. Inc.
-
CHUNHACHART Orawan
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University
-
HANAYAMA Tatsuhiro
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University
-
HIDESAKI Momoe
Processed Food Development and Technology Center, Food Products Company, Ajinomoto Co., Inc.
-
TAHARA Yasutaka
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University
-
Hidesaki Momoe
Processed Food Development And Technology Center Food Products Company Ajinomoto Co. Inc.
-
Tahara Yasutaka
Department Of Applied Biological Chemistry Faculty Of Aglriculture
-
Hanayama Tatsuhiro
Department Of Applied Biological Chemistry Faculty Of Agriculture Shizuoka University
-
Chunhachart Orawan
Department Of Applied Biological Chemistry Faculty Of Agriculture Shizuoka University
-
Tahara Yasutaka
Dep. Of Applied Biological Chemistry Fac. Of Agriculture Shizuoka Univ.
関連論文
- Structure of the Hydrolyzed Product (F-2) Released from γ-Polyglutamic Acid by γ-Glutamyl Hydrolase YwtD of Bacillus subtilis
- Characterization of γ-Glutamyl Hydrolase Produced by Bacillus sp. Isolated from Thai Thua-nao
- Efficient Production of γ-Polyglutamic Acid by Bacillus subtilis (natto) in Jar Fermenters
- Phylogenetic Relationships of Species of the Genus Saccharomyces MEYEN ex REESS Deduced from Partial Base Sequences of 18S and 26S Ribosomal RNAs (Saccharomycetaceae)
- Phylogenetic Relationships of Species of the Genus Kluyveromyces VAN DER WALT (Saccharomycetaceae) Deduced from the Partial Sequences of 18S and 26S Ribosomal RNAs
- Deoxyribonucleic Acid Homologies in Strains of Gluconobacter Species : Taxonomic Studies on Acetic Acid Bacteria and Allied Organisms. Part VIII.
- Ameyamaea chiangmaiensis gen. nov., sp. nov., an Acetic Acid Bacterium in the α-Proteobacteria
- DNA Sequence of Bacillus subtilis (natto) NR-1 γ-Glutamyltranspeptidase Gene, ggt
- Isolation of Glucuronic Acid-containing Glycosphingolipid from Zymomonas mobilis
- Isolation of Zymomonas mobilis Mutant with Increased Tetrahydroxybacteriohopane Content
- IN VITRO ANTIBACTERIAL ACTIVITY OF FA1O3, A NEW QUINOLONE DERIVATIVE OF C-7 POSITION WITH 7-PERHYDRODIAZEPINONE
- Conversion of a Typical Catalase from Bacillus sp.TE124 to a Catalase-Peroxidase by Directed Evolution
- Cloning and High Expression of Catalase Gene from Bacillus sp.TE124
- Ameyamaea chiangmaiensis gen. nov., sp. nov., an Acetic Acid Bacterium in the α-Proteobacteria
- Difference in Transcription Levels of cap Genes for γ-Polyglutamic Acid Production between Bacillus subtilis IFO16449 and Marburg 168
- Isolation of Free Ceramide from Zymomonas mobilis(Microbiology & Fermentation Industry)
- Cloning, Sequencing, and Expression of the Gene from Bacillus circulans That Codes for a Heparinase That Degrades Both Heparin and Heparan Sulfate(Microbiology & Fermentation Technology)
- Purification and Characterization of Heparinase That Degrades Both Heparin and Heparan Sulfate from Bacillus circulans(Microbiology & Fermentation Technology)
- Cloning and Nucleotide Sequence of ApaLI Restriction-modification System from Acetobacter pasteurianus IFO 13753
- Cloning and Nucleotide Sequence of the AgeI Methylase Gene from Agrobacterium gelatinovorum IAM 12617, a Marine Bacterium