AMINO-ACID-SEQUENCE OF ESCHERICHIA-COLI ALKALINE-PHOSPHATASE
AMINO-ACID-SEQUENCE OF ESCHERICHIA-COLI ALKALINE-PHOSPHATASE
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DOI：
10.1073/pnas.78.6.3473
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
WALSH, KA
中科院分区：
文献类型：
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作者：
BRADSHAW, RA;CANCEDDA, F;WALSH, KA
测定了大肠杆菌碱性磷酸酶亚基[正磷酸单酯磷酸水解酶(碱性最适)，EC 3.1.3.1，同工酶3]的完整氨基酸序列。该单体在一个未糖化的多肽链中含有449个氨基酸残基，计算的相对分子质量为47,029。同工酶1在NH2末端有一个额外的精氨酸残基，这可能是由于前体分子的加工过程中的可变性造成的。序列数据来自胰酶和溴化氰多肽及其衍生的其他多肽的手动和自动Edman降解。通过对合适的多肽进行分析，确定了2个二硫键。这种结构证实了早先报道的活性部位丝氨酸以及NH2-和COOH-末端的溴化氰片段周围的序列。二级结构预测将近一半的残基放置在分别具有13%和16%的β-链和β-转角方向的α-螺旋片段中。
The complete amino acid sequence of the E. coli alkaline phosphatase subunit [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1, isozyme 3] was determined. The monomer contains 449 amino acid residues in a single unglycosylated polypeptide chain having a calculated MW of 47,029. Isozyme 1 has an additional arginine residue at the NH2 terminus that presumably results from variability in processing of precursor molecules. Sequence data were obtained from both manual and automatic Edman degradation of the tryptic and cyanogen bromide peptides and other peptides derived from them. The 2 disulfide bonds were determined from analyses of the appropriate peptic peptides. This structure confirms earlier reports of the sequence surrounding the active-site serine and both the NH2- and COOH-terminal cyanogen bromide fragments. A secondary structure prediction places nearly half the residues in .alpha.-helical segments that have 13% and 16%, respectively, in .beta.-strand and .beta.-turn orientations.