Structure of the hydrolyzed product (F-2) released from gamma-polyglutamic acid by gamma-glutamyl hydrolase YwtD of Bacillus subtilis.
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.
Chunhachart
Orawan
O
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Shizuoka, Japan.
Hanayama
Tatsuhiro
T
Hidesaki
Momoe
M
Tanimoto
Hiroyuki
H
Tahara
Yasutaka
Y
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*
C511775:poly(gamma-glutamic acid); D011099:Polyglutamic Acid; D011623:gamma-Glutamyl Hydrolase