Structure of the Hydrolyzed Product (F-2) Released from γ-Polyglutamic Acid by γ-Glutamyl Hydrolase YwtD ofBacillus subtilis
Orawan Chunhachart, Tatsuhiro HANAYAMA, Momoe HIDESAKI, Hiroyuki Tanimoto, Yasutaka Tahara
Abstract
Orawan Chunhachart, Tatsuhiro HANAYAMA, Momoe HIDESAKI, Hiroyuki Tanimoto, Yasutaka Tahara
Abstract
The structure of the hydrolyzed product (F-2) with a molecular mass of about 2 kDa released from gamma-polyglutamic acid by the gamma-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 gamma-glutamyl bond between D- and D-glutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region.
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The structure of the hydrolyzed product (F-2) with a molecular mass of about 2 kDa released from gamma-polyglutamic acid by the gamma-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 gamma-glutamyl bond between D- and D-glutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region.
Key concepts: Polyglutamic acid, Bacillus subtilis, Glutamic acid, Hydrolysis, Chemistry, Hydrolase, Enzyme, Biochemistry