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Comparison Of The Amino Acid Sequence Of L-Mandelate Dehydrogenase From Rhodotorula Graminis With Other L-2-Hydroxyacid Dehydrogenase Enzyme And Its Primary Structure Prediction

机译:红球藻L-扁桃酸脱氢酶氨基酸序列与其他L-2-羟基酸脱氢酶的比较及其一级结构预测

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摘要

A comparison of the primary structure for L-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis with other proteins from the protein databank suggests that there isudsimilarity between this protein and L-2-hydroxyacid dehydrogenase enzymes. R. graminis LMDH exhibits 26–42% identity to L-lactate dehydrogenase from Saccharomyces cerevisiae, L-lactate dehydrogenase from Hansenula anomala, glycolate oxidase from spinach, L-lactate dehydrogenase from Escherichia coli, L-mandelate dehydrogenase from Pseudomonas putida and lactate-2-monooxygenase from Mycobacterium smegmatis. Structurally conserved amino acids are predicted from LMDH sequences corresponding to important regions of the cytochrome and FMN-binding domain defined from the known three-dimensional structure of the L-lactate dehydrogenase from Saccharomyces cerevisiae.
机译:将红假单胞菌的L-扁桃酸脱氢酶(L-MDH)的一级结构与蛋白质数据库中的其他蛋白质进行比较,表明该蛋白质与L-2-羟酸脱氢酶之间存在相似性。 R. graminis LMDH与酿酒酵母的L-乳酸脱氢酶,汉逊酵母中的L-乳酸脱氢酶,菠菜中的乙醇酸氧化酶,大肠杆菌的L-乳酸脱氢酶,假单胞菌的L-扁桃酸脱氢酶表现出26-42%的同一性。来自耻垢分枝杆菌的-2-单加氧酶。根据与啤酒酵母L-乳酸脱氢酶的已知三维结构定义的细胞色素和FMN结合结构域的重要区域相对应的LMDH序列,可预测结构保守的氨基酸。

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