Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase of A1 Drosophila melanogaster

K. Fujimoto, N. Okino, S. I. Kawabata, S. Iwanaga, E. Ohnishi

研究成果: ジャーナルへの寄稿記事

128 引用 (Scopus)

抄録

Clones encoding pro-phenol oxidase [pro-PO; zymogen of phenol oxidase (monophenol, L-dopa:oxygen oxidoreductase, EC 1.14.18.1)] A1 were isolated from a λgt10 library that originated from Drosophila melanogaster strain Oregon-R male adults. The 2294 bp of the cDNA included a 13-bp 5'-noncoding region, a 2070-bp encoding open reading frame of 690 amino acids, and a 211- bp 3'-noncoding region. A hydrophobic NH2-terminal sequence for a signal peptide is absent in the protein. Furthermore, there are six potential N- glycosylation sites in the sequence, but no amino sugar was detected in the purified protein by amino acid analysis, indicating the lack of an N-linked sugar chain. The potential copper-binding sites, amino acids 200-248 and 359- 414, are highly homologous to the corresponding sites of hemocyanin of the tarantula Eurypelma californicum, the horseshoe crab Limulus polyphemus, and the spiny lobster Panulirus interruptus. On the basis of the phylogenetic tree constructed by the neighbor-joining method, vertebrate tyrosinases and molluscan hemocyanins constitute one family, whereas pro-POs and arthropod hemocyanins group with another family. It seems, therefore, likely that pro- PO originates from a common ancestor with arthropod hemocyanins, independently to the vertebrate and microbial tyrosinases.

元の言語英語
ページ(範囲)7769-7773
ページ数5
ジャーナルProceedings of the National Academy of Sciences of the United States of America
92
発行部数17
DOI
出版物ステータス出版済み - 8 31 1995
外部発表Yes

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Enzyme Precursors
Monophenol Monooxygenase
Drosophila melanogaster
Hemocyanin
Complementary DNA
Palinuridae
Horseshoe Crabs
Arthropods
Amino Acids
Vertebrates
Amino Sugars
Protein Sorting Signals
Glycosylation
Open Reading Frames
Libraries
Copper
Proteins
Clone Cells
Binding Sites

All Science Journal Classification (ASJC) codes

  • General

これを引用

Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase of A1 Drosophila melanogaster. / Fujimoto, K.; Okino, N.; Kawabata, S. I.; Iwanaga, S.; Ohnishi, E.

:: Proceedings of the National Academy of Sciences of the United States of America, 巻 92, 番号 17, 31.08.1995, p. 7769-7773.

研究成果: ジャーナルへの寄稿記事

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abstract = "Clones encoding pro-phenol oxidase [pro-PO; zymogen of phenol oxidase (monophenol, L-dopa:oxygen oxidoreductase, EC 1.14.18.1)] A1 were isolated from a λgt10 library that originated from Drosophila melanogaster strain Oregon-R male adults. The 2294 bp of the cDNA included a 13-bp 5'-noncoding region, a 2070-bp encoding open reading frame of 690 amino acids, and a 211- bp 3'-noncoding region. A hydrophobic NH2-terminal sequence for a signal peptide is absent in the protein. Furthermore, there are six potential N- glycosylation sites in the sequence, but no amino sugar was detected in the purified protein by amino acid analysis, indicating the lack of an N-linked sugar chain. The potential copper-binding sites, amino acids 200-248 and 359- 414, are highly homologous to the corresponding sites of hemocyanin of the tarantula Eurypelma californicum, the horseshoe crab Limulus polyphemus, and the spiny lobster Panulirus interruptus. On the basis of the phylogenetic tree constructed by the neighbor-joining method, vertebrate tyrosinases and molluscan hemocyanins constitute one family, whereas pro-POs and arthropod hemocyanins group with another family. It seems, therefore, likely that pro- PO originates from a common ancestor with arthropod hemocyanins, independently to the vertebrate and microbial tyrosinases.",
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T1 - Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase of A1 Drosophila melanogaster

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AU - Ohnishi, E.

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