title: Structure of the hydrolyzed product (F-2) released from gamma-polyglutamic acid by gamma-glutamyl hydrolase YwtD of Bacillus subtilis.
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.
authors.affiliation: Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Shizuoka, Japan.
authors.forename: Orawan
authors.initials: O
authors.lastname: Chunhachart
authors.forename: Tatsuhiro
authors.initials: T
authors.lastname: Hanayama
authors.forename: Momoe
authors.initials: M
authors.lastname: Hidesaki
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Tanimoto
authors.forename: Yasutaka
authors.initials: Y
authors.lastname: Tahara
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology / Q000378:metabolism*; D002850:Chromatography, Gel; D008970:Molecular Weight; D011099:Polyglutamic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D011623:gamma-Glutamyl Hydrolase / Q000378:metabolism*
chemical_list: C511775:poly(gamma-glutamic acid); D011099:Polyglutamic Acid; D011623:gamma-Glutamyl Hydrolase