The structure of L-amino-acid ligase from Bacillus licheniformis.
The structure of L-amino-acid ligase from Bacillus licheniformis.
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地衣芽孢杆菌 L-氨基酸连接酶的结构。
DOI：
10.1107/s0907444912038103
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
J. Saito
中科院分区：
文献类型：
--
作者：
Michihiko Suzuki;Yuichi Takahashi;A. Noguchi;Toshinobu Arai;M. Yagasaki;K. Kino;J. Saito
L-氨基酸连接酶(LALS)是一种通过连接两个L氨基酸来催化形成二肽的酶。虽然许多二肽已知并有望具有医疗和营养价值，但由于其可获得性低和成本高，其实际应用受到限制。LAL可能是高效生产二肽的理想工具；然而，LAL识别底物的分子基础尚未被充分阐明，以设计出理想的二肽LAL。本文用多波长反常色散方法测定了地衣芽孢杆菌NBRC 12200菌株LAL BL00235的晶体结构。BL00235的整体结构与YwfE非常相似，YwfE是唯一一个结构已知的LAL，但催化中心附近的结构存在一些显著的差异。BL00235和YwfE的详细结构比较揭示了底物特异性的分子基础。
L-Amino-acid ligases (LALs) are enzymes which catalyze the formation of dipeptides by linking two L-amino acids. Although many dipeptides are known and expected to have medical and nutritional benefits, their practical use has been limited owing to their low availability and high expense. LALs are potentially desirable tools for the efficient production of dipeptides; however, the molecular basis of substrate recognition by LAL has not yet been sufficiently elucidated for the design of ideal LALs for the desired dipeptides. This report presents the crystal structure of the LAL BL00235 derived from Bacillus licheniformis NBRC 12200 determined at 1.9 Å resolution using the multi-wavelength anomalous dispersion method. The overall structure of BL00235 is fairly similar to that of YwfE, the only LAL with a known structure, but the structure around the catalytic site contains some significant differences. Detailed structural comparison of BL00235 with YwfE sheds some light on the molecular basis of the substrate specificities.
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影响因子：
5.1
作者：
Fawaz MV;Topper ME;Firestine SM
通讯作者：
Firestine SM
影响因子：
2.9
作者：
LEMASTER, DM;RICHARDS, FM
通讯作者：
RICHARDS, FM
影响因子：
56.9
作者：
FAN, C;MOEWS, PC;KNOX, JR
通讯作者：
KNOX, JR
影响因子：
2.9
作者：
Thoden, JB;Kappock, TJ;Holden, HM
通讯作者：
Holden, HM