Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase.

T. Joh, H. Takeshima, Teruhisa Tsuzuki, C. Setoyama, K. Shimada, S. Tanase, S. Kuramitsu, H. Kagamiyama, Y. Morino

研究成果: ジャーナルへの寄稿記事

54 引用 (Scopus)

抄録

A cDNA clone, named ppcMDH-1 and covering a part of the coding region for the porcine cytosolic malate dehydrogenase (cMDH) mRNA, was isolated from a porcine liver cDNA library. Subsequently, mouse cMDH cDNA clones were isolated from mouse liver and heart cDNA libraries, using the ppcMDH-1 cDNA as a probe. The longest clone, named pmcMDH-5, was sequenced and the primary structure of the mouse cMDH deduced from its cDNA sequence showed that the mouse cMDH consists of the 334-amino acid residues. When the amino acid sequence of the mouse cMDH was compared with that of the porcine cMDH, they shared a 93% homology. On the other hand, the amino acid sequences of mouse cMDH and mitochondrial MDH (mMDH) showed about 23% overall homology. Surprisingly, comparison of the amino acid sequences among the mammalian and bacterial MDHs revealed that the homology between the mouse cMDH and thermophilic bacterial MDH, as well as the homology between the mouse mMDH and Escherichia coli MDH, markedly exceeds the intraspecies sequence homology between mMDH and cMDH from mice.

元の言語英語
ページ(範囲)15127-15131
ページ数5
ジャーナルThe Journal of biological chemistry
262
発行部数31
出版物ステータス出版済み - 1 1 1987

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Malate Dehydrogenase
Cloning
Sequence Analysis
Organism Cloning
Amino Acid Sequence
Complementary DNA
Amino Acids
Swine
Clone Cells
Gene Library
Liver
Sequence Homology
Escherichia coli
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. / Joh, T.; Takeshima, H.; Tsuzuki, Teruhisa; Setoyama, C.; Shimada, K.; Tanase, S.; Kuramitsu, S.; Kagamiyama, H.; Morino, Y.

:: The Journal of biological chemistry, 巻 262, 番号 31, 01.01.1987, p. 15127-15131.

研究成果: ジャーナルへの寄稿記事

Joh, T, Takeshima, H, Tsuzuki, T, Setoyama, C, Shimada, K, Tanase, S, Kuramitsu, S, Kagamiyama, H & Morino, Y 1987, 'Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase.', The Journal of biological chemistry, 巻. 262, 番号 31, pp. 15127-15131.
Joh, T. ; Takeshima, H. ; Tsuzuki, Teruhisa ; Setoyama, C. ; Shimada, K. ; Tanase, S. ; Kuramitsu, S. ; Kagamiyama, H. ; Morino, Y. / Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. :: The Journal of biological chemistry. 1987 ; 巻 262, 番号 31. pp. 15127-15131.
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abstract = "A cDNA clone, named ppcMDH-1 and covering a part of the coding region for the porcine cytosolic malate dehydrogenase (cMDH) mRNA, was isolated from a porcine liver cDNA library. Subsequently, mouse cMDH cDNA clones were isolated from mouse liver and heart cDNA libraries, using the ppcMDH-1 cDNA as a probe. The longest clone, named pmcMDH-5, was sequenced and the primary structure of the mouse cMDH deduced from its cDNA sequence showed that the mouse cMDH consists of the 334-amino acid residues. When the amino acid sequence of the mouse cMDH was compared with that of the porcine cMDH, they shared a 93{\%} homology. On the other hand, the amino acid sequences of mouse cMDH and mitochondrial MDH (mMDH) showed about 23{\%} overall homology. Surprisingly, comparison of the amino acid sequences among the mammalian and bacterial MDHs revealed that the homology between the mouse cMDH and thermophilic bacterial MDH, as well as the homology between the mouse mMDH and Escherichia coli MDH, markedly exceeds the intraspecies sequence homology between mMDH and cMDH from mice.",
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AU - Joh, T.

AU - Takeshima, H.

AU - Tsuzuki, Teruhisa

AU - Setoyama, C.

AU - Shimada, K.

AU - Tanase, S.

AU - Kuramitsu, S.

AU - Kagamiyama, H.

AU - Morino, Y.

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N2 - A cDNA clone, named ppcMDH-1 and covering a part of the coding region for the porcine cytosolic malate dehydrogenase (cMDH) mRNA, was isolated from a porcine liver cDNA library. Subsequently, mouse cMDH cDNA clones were isolated from mouse liver and heart cDNA libraries, using the ppcMDH-1 cDNA as a probe. The longest clone, named pmcMDH-5, was sequenced and the primary structure of the mouse cMDH deduced from its cDNA sequence showed that the mouse cMDH consists of the 334-amino acid residues. When the amino acid sequence of the mouse cMDH was compared with that of the porcine cMDH, they shared a 93% homology. On the other hand, the amino acid sequences of mouse cMDH and mitochondrial MDH (mMDH) showed about 23% overall homology. Surprisingly, comparison of the amino acid sequences among the mammalian and bacterial MDHs revealed that the homology between the mouse cMDH and thermophilic bacterial MDH, as well as the homology between the mouse mMDH and Escherichia coli MDH, markedly exceeds the intraspecies sequence homology between mMDH and cMDH from mice.

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