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酪氨酸酚裂解酶的结晶及晶体数据。

Crystallization and crystal data on tyrosine phenol-lyase.

作者信息

Demidkina T V, Myagkikh I V, Antson A A, Harutyunyan E H

机构信息

Institute of Molecular Biology, USSR Academy of Sciences, Moscow.

出版信息

FEBS Lett. 1988 May 23;232(2):381-2. doi: 10.1016/0014-5793(88)80774-9.

DOI:10.1016/0014-5793(88)80774-9
PMID:3378628
Abstract

Crystals of the apoenzyme of tyrosine phenol-lyase (EC 4.1.99.2), a pyridoxal 5'-phosphate-dependent enzyme from Citrobacter intermedius, have been grown by vapor diffusion of an ammonium sulfate solution to a protein solution. The crystals belong to space group P2(1)2(1)2, with dimensions of a = 75.5 A, b = 138.4 A and c = 94.1 A and diffract up to 2.7 A resolution. The asymmetric unit contains one half of the enzyme tetrameric molecule. Two heavy-atom derivatives of the crystals have been obtained.

摘要

来自中间柠檬酸杆菌的一种依赖于磷酸吡哆醛的酪氨酸酚裂解酶(EC 4.1.99.2)的脱辅基酶晶体,通过硫酸铵溶液向蛋白质溶液的气相扩散法生长而成。这些晶体属于空间群P2(1)2(1)2,晶胞参数a = 75.5 Å,b = 138.4 Å,c = 94.1 Å,衍射分辨率高达2.7 Å。不对称单元包含酶四聚体分子的一半。已获得该晶体的两种重原子衍生物。

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2
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引用本文的文献

1
Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions.脱辅基和全酶形式的酪氨酸酚裂解酶结构揭示了一种催化关键的闭合构象,并提出了钾离子激活的机制。
Biochemistry. 2006 Jun 20;45(24):7544-52. doi: 10.1021/bi0601858.