哺乳动物组氨酸脱羧酶和鸟氨酸脱羧酶之间结构-活性特征共性的实验证据。
Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase.
作者信息
Engel N, Olmo M T, Coleman C S, Medina M A, Pegg A E, Sánchez-Jiménez F
机构信息
Laboratorio de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Málaga, Spain.
出版信息
Biochem J. 1996 Dec 1;320 ( Pt 2)(Pt 2):365-8. doi: 10.1042/bj3200365.
Abstract
Common protein motifs between histidine decarboxylase (HDC) and ornithine decarboxylase (ODC) were detected by computational analysis. Mutants were generated and expressed in vitro. In both enzymes, terminal PEST-region-containing fragments are not essential for decarboxylation (PEST regions are sequence fragments enriched in proline, glutamic acid, serine and threonine residues in a hydrophilic fragment flanked by cationic amino acids). The substitution of a very well conserved histidine residue by alanine causes a severalfold increase of the apparent K(m) values for the respective substrates.
摘要
通过计算分析检测到组氨酸脱羧酶（HDC）和鸟氨酸脱羧酶（ODC）之间的常见蛋白质基序。生成突变体并在体外进行表达。在这两种酶中，含末端PEST区域的片段对于脱羧反应并非必需（PEST区域是在由阳离子氨基酸侧翼的亲水性片段中富含脯氨酸、谷氨酸、丝氨酸和苏氨酸残基的序列片段）。用丙氨酸替代一个高度保守的组氨酸残基会导致各自底物的表观K(m)值增加数倍。
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