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Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution.

作者信息

Kamitori S, Hirotsu K, Higuchi T, Kondo K, Inoue K, Kuramitsu S, Kagamiyama H, Higuchi Y, Yasuoka N, Kusunoki M

机构信息

Department of Chemistry, Faculty of Science, Osaka City University.

出版信息

J Biochem. 1988 Sep;104(3):317-8. doi: 10.1093/oxfordjournals.jbchem.a122464.

DOI:10.1093/oxfordjournals.jbchem.a122464
PMID:3071527
Abstract

The crystal structure of aspartate aminotransferase of Escherichia coli was determined by X-ray structure analysis at 2.8 A resolution. The structure was solved by the molecular replacement method and refined to an R-factor of 0.27, and it was found that the overall structure of AspAT of E. coli is similar to that of those of higher animals.

摘要

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Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase.
脱羧酶中磷酸吡哆醛-5'-磷酸结合的结构基序:基于乳酸杆菌30a鸟氨酸脱羧酶晶体结构的分析。
Protein Sci. 1995 May;4(5):849-54. doi: 10.1002/pro.5560040504.
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A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level.5'-磷酸吡哆醛依赖性脱羧酶与转氨酶在分子水平上的比较。
Experientia. 1991 Dec 1;47(11-12):1104-18. doi: 10.1007/BF01918374.