TY - JOUR
T1 - Novel diketopiperazine metabolism in a microorganism
T2 - Two-step hydrolysis of cyclo(Gly-Leu) to amino acids and preliminary characterization of cyclo(Gly-Leu) hydrolase and dipeptidase
AU - Kanzaki, Hiroshi
AU - Mizuta, Naoki
AU - Nitoda, Teruhiko
AU - Kawazu, Kazuyoshi
N1 - Funding Information:
We thank Prof. Hidenori Yamada of the Faculty of Engineering, Okayama University for quantitative analysis of peptides with a Hitachi 835 amino acid analyzer. We are grateful to the SC-NMR laboratory of Okayama University and the MS laboratory of the Faculty of Agriculture. Okavama University for ‘H-NMR and MS experiments, Qespectivdly. This work was Supported in part by a Grant-in-Aid for Scientific Research (No. 09660095) from the Japanese Ministry of Education, Science, Sports and Culture to HK.
PY - 2000
Y1 - 2000
N2 - A bacterium, strain NM 5-3, isolated from soil exhibited the highest cyclo(Gly-Leu) (CGL)-hydrolyzing activity and was identified as Agrobacterium radiobacter. The reaction products from CGL were dipeptides (Leu-Gly and Gly-Leu) and amino acids (Leu and Gly). Inhibitors for the dipeptidase of this strain did not inhibit the hydrolysis of CGL to dipeptides, indicating that two distinct enzymes, CGLase and a dipeptidase, were involved in its hydrolysis. The activities of these two enzymes were separated by anion-exchange column chromatography. The results indicated that strain NM5-3 hydrolyzed CGL via the dipeptides to the corresponding amino acids. The CGLase fraction was found to catalyze the hydrolysis of cyclo(Gly-D-Leu), cyclo(Gly-Gly), cyclo(L-Ala-Gly), and cyclo(D-Ala-Gly). On the other hand, the dipeptidase fraction exhibited L-specific substrate specificity.
AB - A bacterium, strain NM 5-3, isolated from soil exhibited the highest cyclo(Gly-Leu) (CGL)-hydrolyzing activity and was identified as Agrobacterium radiobacter. The reaction products from CGL were dipeptides (Leu-Gly and Gly-Leu) and amino acids (Leu and Gly). Inhibitors for the dipeptidase of this strain did not inhibit the hydrolysis of CGL to dipeptides, indicating that two distinct enzymes, CGLase and a dipeptidase, were involved in its hydrolysis. The activities of these two enzymes were separated by anion-exchange column chromatography. The results indicated that strain NM5-3 hydrolyzed CGL via the dipeptides to the corresponding amino acids. The CGLase fraction was found to catalyze the hydrolysis of cyclo(Gly-D-Leu), cyclo(Gly-Gly), cyclo(L-Ala-Gly), and cyclo(D-Ala-Gly). On the other hand, the dipeptidase fraction exhibited L-specific substrate specificity.
KW - Diketopiperazine-hydrolyzing enzyme
KW - Dipeptidase
KW - Enrichment culture
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U2 - 10.1016/S1389-1723(00)80064-X
DO - 10.1016/S1389-1723(00)80064-X
M3 - Article
C2 - 16232805
AN - SCOPUS:0034210620
SN - 1389-1723
VL - 89
SP - 602
EP - 605
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 6
ER -