Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase
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- 作者：Jiang Wena ; b ; Cristina Nowickic ; cnowicki@qb.ffyb.uba.ar" class="auth_mail" title="E-mail the corresponding author ; Wulf Blankenfeldtb ; wulf.blankenfeldt@helmholtz-hzi.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：Leishmaniasis ; Metabolism ; Transamination ; Aminotransferase ; Substrate specificity ; Drug design
- 刊名：Molecular & Biochemical Parasitology
- 出版年：2015
- 出版时间：August 2015
- 年：2015
- 卷：202
- 期：2
- 页码：34-37
- 全文大小：1203 K
文摘
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LmexBSAT transaminates aromatic amino acids and aspartate, but not glutamate.
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Its efficiency with 2-oxoglutarate suggests involvement in glutamate production.
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The crystal structure of LmexBSAT was determined at 1.91 Å resolution.
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Similarity to the closed form of ASATs explains preference for Asp versus Glu.
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Flexibility of R291 explains capability of accepting aromatic amino acids.