The Amino Acid Sequence of Ascorbate Peroxidase from Tea Has a High Degree of Homology to That of Cytochrome c Peroxidase from Yeast
The Amino Acid Sequence of Ascorbate Peroxidase from Tea Has a High Degree of Homology to That of Cytochrome c Peroxidase from Yeast
复制标题
茶叶抗坏血酸过氧化物酶的氨基酸序列与酵母细胞色素c过氧化物酶具有高度同源性
DOI:
10.1093/oxfordjournals.pcp.a078228
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发表时间:
1992
影响因子:
4.9
通讯作者:
K. Asada
中科院分区:
文献类型:
--
作者:
Gong;S. Sano;K. Asada
The chloroplast isozyme of ascorbate peroxidase from tea leaves was digested with lysyl endopeptidase, and the amino acid sequences of the peptide fragments were determined. These sequences accounted for 64% of the amino acids in the entire protein. The sequence of one of the peptides can be aligned with the region which includes the proximal histidine that serves as the fifth ligand of the heme iron in guaiacol peroxidases and cytochromecperoxidase. The sequences of the peptides from ascorbate peroxidase exhibit a higher degree of homology to the sequence of cytochromecperoxidase from yeast than to those of guaiacol peroxidases from plants. In addition, three of the peptides from ascorbate peroxidase show a high degree of homology to triose-phosphate isomerase from maize. From the available amino acid sequences and the enzymatic and molecular properties of ascorbate and cytochromecperoxidases, we propose that these hydrogen peroxide-scavenging peroxidases that use either cytochromecor ascorbate as the electron donor originated from the same ancestral protein.