TY - JOUR
T1 - Occurrence of D-amino acids and a pyridoxal 5′-phosphate-dependent aspartate racemase in the acidothermophilic archaeon, Thermoplasma acidophilum
AU - Long, Zhiqun
AU - Lee, Jen Ai
AU - Okamoto, Taizo
AU - Sekine, Masae
AU - Nimura, Noriyuki
AU - Imai, Kazuhiro
AU - Yohda, Masafumi
AU - Maruyama, Tadashi
AU - Sumi, Masato
AU - Kamo, Naoki
AU - Yamagishi, Akihiko
AU - Oshima, Tairo
AU - Homma, Hiroshi
N1 - Funding Information:
The authors thank Tosoh Co. (Tokyo, Japan) and Sumika Chemical Analysis Service (Osaka, Japan) for the generous gifts of the reverse-phase column (ODS-M80) and the chiral column (OA2500S), respectively. This work was supported, in part, by a Grant-in-Aid for postdoctoral foreign researchers in Japan P99179 (to Z.L.) from the Japan Society for the promotion of Science. Additional grant supports was provided by the Ministry of Education, Science, Sports and Culture of Japan (Grants-in-Aid for Scientific Research 11672163 (to H.H.) and 09460053 (to M.Y.)), the Fugaku Trust for Medical Reserch, and the Fujisawa Foundation.
PY - 2001
Y1 - 2001
N2 - Free D-amino acid content in some archaea was investigated and D-forms of several amino acids were found in them. In the acidothermophilic archaeon, Thermoplasma acidophilum, the proportion of D-aspartate (D-Asp) to total Asp was as high as 39.7%. Crude extracts of Thermoplasma acidophilum had Asp-specific racemase activity that was pyridoxal 5′-phosphate (PLP)-dependent. The relative insensitivity to a SH-modifying reagent distinguished this activity from those of the PLP-independent Asp racemases found in other hyperthermophilic archaea (Matsumoto, M., et al., J. Bacteriol. 181, 6560-6563 1999). Thus, high levels of D-Asp should be produced by a new type(s) of Asp-specific racemase in Thermoplasma acidophilum, although the function of D-Asp in this archaeon remains unknown.
AB - Free D-amino acid content in some archaea was investigated and D-forms of several amino acids were found in them. In the acidothermophilic archaeon, Thermoplasma acidophilum, the proportion of D-aspartate (D-Asp) to total Asp was as high as 39.7%. Crude extracts of Thermoplasma acidophilum had Asp-specific racemase activity that was pyridoxal 5′-phosphate (PLP)-dependent. The relative insensitivity to a SH-modifying reagent distinguished this activity from those of the PLP-independent Asp racemases found in other hyperthermophilic archaea (Matsumoto, M., et al., J. Bacteriol. 181, 6560-6563 1999). Thus, high levels of D-Asp should be produced by a new type(s) of Asp-specific racemase in Thermoplasma acidophilum, although the function of D-Asp in this archaeon remains unknown.
UR - https://www.scopus.com/pages/publications/0034808464
UR - https://www.scopus.com/pages/publications/0034808464#tab=citedBy
U2 - 10.1006/bbrc.2001.4353
DO - 10.1006/bbrc.2001.4353
M3 - Article
C2 - 11181048
AN - SCOPUS:0034808464
SN - 0006-291X
VL - 281
SP - 317
EP - 321
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -