TY - JOUR
T1 - Enzymatic dehydrogenation of cyclo(L-Phe-L-Leu) to a bioactive derivative, albonoursin
AU - Kanzaki, Hiroshi
AU - Imura, Daisuke
AU - Nitoda, Teruhiko
AU - Kawazu, Kazuyoshi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture to HK. We are grateful to the SC–NMR laboratory of Okayama University and the MS laboratory of the Faculty of Agriculture, Okayama University for assistance in the -NMR and MS experiments, respectively.
PY - 1999/3/11
Y1 - 1999/3/11
N2 - The cell-free extract of Streptomyces sp. KO-2388, an albonoursin- producing strain, was found to catalyze the conversion of cyclo(L-Phe-L-Leu) to albonoursin. The conversion activity was simply determined by measuring the increase in ultraviolet (UV) absorption of the reaction mixture at 317 nm, λ(max) (ε 25,400) of albonoursin, where cyclo(L-Phe-L-Leu) had no absorption. The optimum pH and temperature of this bioconversion using the cell-free extract were determined to be pH 8.0-9.5 and 60°C, respectively. Under the optimum conditions, 620 mg/l of albonoursin was obtained with a conversion ratio of 62% after 24 h incubation.
AB - The cell-free extract of Streptomyces sp. KO-2388, an albonoursin- producing strain, was found to catalyze the conversion of cyclo(L-Phe-L-Leu) to albonoursin. The conversion activity was simply determined by measuring the increase in ultraviolet (UV) absorption of the reaction mixture at 317 nm, λ(max) (ε 25,400) of albonoursin, where cyclo(L-Phe-L-Leu) had no absorption. The optimum pH and temperature of this bioconversion using the cell-free extract were determined to be pH 8.0-9.5 and 60°C, respectively. Under the optimum conditions, 620 mg/l of albonoursin was obtained with a conversion ratio of 62% after 24 h incubation.
KW - Bioconversion
KW - Cyclic dipeptide
KW - Dehydrodiketopiprazines
KW - Dioxopiperazine
KW - Piprazinedione
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U2 - 10.1016/S1381-1177(98)00079-4
DO - 10.1016/S1381-1177(98)00079-4
M3 - Article
AN - SCOPUS:0033545547
VL - 6
SP - 265
EP - 270
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
SN - 1381-1177
IS - 3
ER -