粗糙脉孢菌NADP特异性谷氨酸脱氢酶的氨基酸序列。
Amino-acid sequence of NADP-specific glutamate dehydrogenase of neurospora crassa.
作者信息
Wootton J C, Chambers G K, Holder A A, Baron A J, Taylor J G, Fincham J R, Blumenthal K M, Moon K, Smith E L
出版信息
Proc Natl Acad Sci U S A. 1974 Nov;71(11):4361-5. doi: 10.1073/pnas.71.11.4361.
Abstract
A tentative primary structure of the NADP-specific glutamate dehydrogenase [L-glutamate: NADP oxidoreductase (deaminating), EC 1.4.1.4] from Neurospora crassa has been determined. The proposed sequence contains 452 amino-acid residues in each of the identical subunits of the hexameric enzyme. Comparison of the sequence with that of the bovine liver enzyme reveals considerable homology in the amino-terminal portion of the chain, including the vicinity of the reactive lysine, with only shorter stretches of homology within the carboxyl-terminal regions. The significance of this distribution of homologous regions is discussed.
摘要
粗糙脉孢菌中NADP特异性谷氨酸脱氢酶[L-谷氨酸：NADP氧化还原酶（脱氨基），EC 1.4.1.4]的初步一级结构已被确定。所提出的序列在六聚体酶的每个相同亚基中包含452个氨基酸残基。将该序列与牛肝酶的序列进行比较，发现在链的氨基末端部分有相当大的同源性，包括反应性赖氨酸附近，而在羧基末端区域内只有较短的同源片段。讨论了同源区域这种分布的意义。
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