Otto J, Argos P, Rossmann M G
Eur J Biochem. 1980 Aug;109(2):325-30. doi: 10.1111/j.1432-1033.1980.tb04798.x.
The secondary structure of glycerol-3-phosphate dehydrogenase was predicted from its amino acid sequence. The pattern of helices and sheets within the first half of the polypeptide as well as specific marker residues were consistent with the properties of the NAD binding domain in other dehydrogenases. The second half of the sequence shows similarities with the catalytic domain of glyceraldehyde-3-phosphate dehydrogenase. The resulting two-domain structure of glycerol-3-phosphate dehydrogenase allows the correct environment for the B specificity of the nicotinamide ring and the L-glycerol 3-phosphate substrate.
通过甘油-3-磷酸脱氢酶的氨基酸序列预测了其二级结构。多肽前半部分的螺旋和折叠模式以及特定的标记残基与其他脱氢酶中NAD结合结构域的特性一致。序列的后半部分与甘油醛-3-磷酸脱氢酶的催化结构域相似。由此产生的甘油-3-磷酸脱氢酶的双结构域结构为烟酰胺环的B特异性和L-甘油3-磷酸底物提供了合适的环境。
