Differences in charge and kinetic properties of alcohol dehydrogenase 4 from C57BL/6 mice compared to other inbred strains are associated with a cysteine120 to arginine120 substitution.

Differences in charge and kinetic properties of alcohol dehydrogenase 4 from C57BL/6 mice compared to other inbred strains are associated with a cysteine120 to arginine120 substitution.
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与其他近交系小鼠相比,C57BL/6 小鼠的乙醇脱氢酶 4 的电荷和动力学特性差异与半胱氨酸 120 替换为精氨酸 120 相关。

DOI:
10.1023/a:1010278631535
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发表时间:
2001
影响因子:
2.4
通讯作者:
Felder,MR
Felder,MR
中科院分区:
生物学4区
文献类型:
--
作者:
Dolney,DE;Szalai,G;Felder,MR

文献摘要

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IV 类乙醇脱氢酶 (ADH4) 参与视黄醇代谢,主要在小鼠的眼、消化和生殖组织中表达。与其他非 C57BJ/6J 品系相比,C57BL/6J 小鼠中天然存在的遗传变异导致 ADH4 酶在电泳过程中迁移速度更快。与 C3HeB/FeJ 小鼠的基因相比,发现 C57BL/6ADH4 基因编码序列有两个核苷酸取代。外显子5中的取代编码C57BL/6 ADH4多肽中的Arg120而不是Cys120;这可以解释蛋白质电泳表型。 Arg120 存在于所有已发表的哺乳动物 ADH4 序列中,但仅存在于有限数量的小鼠品系中。 Arg120 残基是底物结合袋外环的一部分,似乎对酶对多种底物的亲和力有影响。
Alcohol dehydrogenase class IV (ADH4) participates in retinol metabolism and is expressed primarily in ocular, digestive, and reproductive tissues of the mouse. A naturally occurring genetic variant in C57BL/6J mice results in a faster migrating ADH4 enzyme during electrophoresis when compared to other non-C57BJ/6J strains. The C57BL/6ADH4gene coding sequence is found to have two nucleotide substitutions when compared to the gene from C3HeB/FeJ mice. The substitution in exon 5 encodes Arg120 instead of Cys120 in C57BL/6 ADH4 polypeptide; that would account for the protein electrophoretic phenotype. Arg120 is present in all published mammalian ADH4 sequences but is only in a limited number of mouse strains. The Arg120 residue is part of the outer loop of the substrate binding pocket and appears to have an effect on the affinity of the enzyme for several substrates.