牛肝谷氨酸脱氢酶：暂定氨基酸序列；活性赖氨酸的鉴定；特定酪氨酸的硝化以及三磷酸鸟苷变构抑制作用的丧失
Bovine liver glutamate dehydrogenase: tentative amino acid sequence; identification of a reactive lysine; nitration of a specific tyrosine and loss of allosteric inhibition by guanosine triphosphate.
作者信息
Smith E L, Landon M, Piszkiewicz D, Brattin W J, Langley T J, Melamed M D
出版信息
Proc Natl Acad Sci U S A. 1970 Oct;67(2):724-30. doi: 10.1073/pnas.67.2.724.
Abstract
A tentative but almost complete amino acid sequence for the subunit peptide chain of bovine liver glutamate dehydrogenase indicates a minimal size of 506 residues with a molecular weight of 56,100, in accord with the physical size of the subunit of 55,900. Inactivation with pyridoxal 5'-phosphate, followed by reduction with sodium borohydride, has permitted identification of the essential lysine as residue 97. Nitration of tyrosine-412 is accompanied by loss of the allosteric inhibitory effect of guanosine triphosphate. Comparison of the sequences of glutamate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase has indicated that only two 12-residue sequences are similar in the two enzymes; this sequence includes reactive lysine-97 of the former enzyme.
摘要
牛肝谷氨酸脱氢酶亚基肽链的氨基酸序列初步确定但几乎完整，表明其最小长度为506个残基，分子量为56,100，这与55,900的亚基物理大小相符。用5'-磷酸吡哆醛使其失活，随后用硼氢化钠还原，已确定必需赖氨酸为第97位残基。酪氨酸-412的硝化伴随着三磷酸鸟苷变构抑制作用的丧失。谷氨酸脱氢酶和3-磷酸甘油醛脱氢酶序列的比较表明，这两种酶中只有两个12个残基的序列相似；该序列包括前一种酶的活性赖氨酸-97。
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