DIHYDROLIPOAMIDE DEHYDROGENASE - FUNCTIONAL SIMILARITIES AND DIVERGENT EVOLUTION OF THE PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASES
DIHYDROLIPOAMIDE DEHYDROGENASE - FUNCTIONAL SIMILARITIES AND DIVERGENT EVOLUTION OF THE PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASES
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DOI：
10.1016/0003-9861(89)90309-3
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发表时间：
1989-02-01
影响因子：
3.9
通讯作者：
PATEL, MS
中科院分区：
文献类型：
--
作者：
CAROTHERS, DJ;PONS, G;PATEL, MS
二氢脂酰胺脱氢酶（E3）是三种α-脂酰胺酶的共同组分。氧化丙酮酸的酮酸脱氢酶复合物，α-酮戊二酸和支链α-酮酸E3还参与甘氨酸裂解系统。E2属于称为吡啶核苷酸-二硫化物氧化还原酶的酶家族，催化吡啶核苷酸和二硫化物化合物之间的电子转移。该综述总结了可从多种物种获得的关于E3的信息，从具有E3但不具有α-E3的嗜盐古细菌获得的信息。酮酸脱氢酶复合物，哺乳动物物种。综述了两种E3同工酶（一种用于丙酮酸脱氢酶复合物，另一种用于α-E3同工酶）存在的证据。酮戊二酸脱氢酶复合物，另一种用于支链α-酮酸脱氢酶复合物）和E3的可能的哺乳动物同工酶，其中一种与三种α-酮酸脱氢酶复合物和一个用于甘氨酸裂解系统。 大肠杆菌、酵母、猪和人的E3的完整氨基酸序列的比较显示某些氨基酸残基或短序列的相当大的同源性，特别是在特定的催化和结构域。在其他几个物种的E3上发现了与有限的可用氨基酸序列信息相似的同源性。还提供了其他成员黄素蛋白的序列比较[例如，谷胱甘肽还原酶和汞（II）还原酶]。根据已知的人谷胱甘肽还原酶的三级结构，有可能预测E3的结构域结构。此外，序列信息可能有助于更好地理解这些黄素蛋白在不同物种中的不同进化关系。
Dihydroliponamide dehydrogenase (E3) is the common component of the three .alpha.-keto-acid dehydrogenase complexes oxidizing pyruvate, .alpha.-ketoglutarate, and the branched-chain .alpha.-ketoacids. E3 also participates in the glycine cleavage system. E2 belongs to the enzyme family called pyridine nucleotide-disulfide oxidoreductases, catalyzing the electron transfer between pyridine nucleotides and disulfide compounds. This review summarizes the information available for E3 from a variety of species, from a halophilic archaebacterium which has E3 but no .alpha.-ketoacid dehydrogenase complexes, to mammalian species. Evidence is reviewed for the existance of two E3 isozymes (one for pyruvate dehydrogenase complex and .alpha.-ketoglutarate dehydrogenase complex and the other for branched-chain .alpha.-ketoacid dehydrogenase complex) in Pseudomonas species and for possible mammalian isozymes of E3, one associated with the three .alpha.-ketoacid dehydrogenase complexes and one for the glycine cleavage system. The comparison of the complete amino acid sequences of E3 from Escherichia coli, yeast, pig, and human shows considerable homologies of certain amino acid residues or short stretches of sequences, especially in the specific catalytic and structural domains. Similar homology is found with the limited available amino acid sequence information on E3 from several other species. Sequence comparison is also presented for other member flavoproteins [e.g., glutathione reductase and mercury (II) reductase] of the pyridine nucleotide-disulfide oxidoreductase family. Based on the known teritiary structure of human glutathione reductase it may be possible to predict the domain structues of E3. Additionally, the sequence information may help to better understand a divergent evolutionary relationship among these flavoproteins in different species.