Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily

Ken Noda; Kunio Shiota; Tomoya Ogawa; Shintaro Yagi; Michio Takahashi

doi:10.1262/jrd.39.169

Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily

Ken Noda, Kunio Shiota, Tomoya Ogawa, Shintaro Yagi, Michio Takahashi

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

We have previously purified the 20±hydroxysteroid dehydrogenase (20±HSD) molecule from normal mature rat ovarian cytosol [Biochim. Biophys. Acta, 1991, 1079: 112-118]. In order to further characterize the 20±HSD and to obtain information for molecular cloning of the enzyme, we determined its N-terminal amino acid sequence. The sequence was shown to be Ser-Lys-lle-Gln-Lys-Met-Glu-Leu-Asn-Asp-Gly-His-Ser-lle-Pro-Val-Leu-Gly-Phe-Xaa-Thr. A search of the SWISS-PROT protein sequence database for N-terminal amino acid sequence similarities revealed 6 highly homologous proteins, including bovine prostaglandin F synthase, rat liver 3±hydroxysteroid dehydrogenase, bovine lens aldose reductase, human aldose reductase, frog 3±crystallin and human liver chlordecone reductase, suggesting that rat ovarian 20ar-HSD belongs to the aldo-keto reductase gene superfamily.

Original language	English
Pages (from-to)	169-173
Number of pages	5
Journal	Journal of Reproduction and Development
Volume	39
Issue number	2
DOIs	https://doi.org/10.1262/jrd.39.169
Publication status	Published - 1993
Externally published	Yes

Keywords

20α-Hydroxy steroid dehydrogenase
Aldo-keto reductase
Automatic Edman degradation
N-terminal amino acid sequence

ASJC Scopus subject areas

Animal Science and Zoology

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10.1262/jrd.39.169

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title = "Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily",

abstract = "We have previously purified the 20±hydroxysteroid dehydrogenase (20±HSD) molecule from normal mature rat ovarian cytosol [Biochim. Biophys. Acta, 1991, 1079: 112-118]. In order to further characterize the 20±HSD and to obtain information for molecular cloning of the enzyme, we determined its N-terminal amino acid sequence. The sequence was shown to be Ser-Lys-lle-Gln-Lys-Met-Glu-Leu-Asn-Asp-Gly-His-Ser-lle-Pro-Val-Leu-Gly-Phe-Xaa-Thr. A search of the SWISS-PROT protein sequence database for N-terminal amino acid sequence similarities revealed 6 highly homologous proteins, including bovine prostaglandin F synthase, rat liver 3±hydroxysteroid dehydrogenase, bovine lens aldose reductase, human aldose reductase, frog 3±crystallin and human liver chlordecone reductase, suggesting that rat ovarian 20ar-HSD belongs to the aldo-keto reductase gene superfamily.",

keywords = "20α-Hydroxy steroid dehydrogenase, Aldo-keto reductase, Automatic Edman degradation, N-terminal amino acid sequence",

author = "Ken Noda and Kunio Shiota and Tomoya Ogawa and Shintaro Yagi and Michio Takahashi",

year = "1993",

doi = "10.1262/jrd.39.169",

language = "English",

volume = "39",

pages = "169--173",

journal = "Journal of Reproduction and Development",

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publisher = "Japanese Society of Animal Reproduction (JSAR)",

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T1 - Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily

AU - Noda, Ken

AU - Shiota, Kunio

AU - Ogawa, Tomoya

AU - Yagi, Shintaro

AU - Takahashi, Michio

PY - 1993

Y1 - 1993

N2 - We have previously purified the 20±hydroxysteroid dehydrogenase (20±HSD) molecule from normal mature rat ovarian cytosol [Biochim. Biophys. Acta, 1991, 1079: 112-118]. In order to further characterize the 20±HSD and to obtain information for molecular cloning of the enzyme, we determined its N-terminal amino acid sequence. The sequence was shown to be Ser-Lys-lle-Gln-Lys-Met-Glu-Leu-Asn-Asp-Gly-His-Ser-lle-Pro-Val-Leu-Gly-Phe-Xaa-Thr. A search of the SWISS-PROT protein sequence database for N-terminal amino acid sequence similarities revealed 6 highly homologous proteins, including bovine prostaglandin F synthase, rat liver 3±hydroxysteroid dehydrogenase, bovine lens aldose reductase, human aldose reductase, frog 3±crystallin and human liver chlordecone reductase, suggesting that rat ovarian 20ar-HSD belongs to the aldo-keto reductase gene superfamily.

AB - We have previously purified the 20±hydroxysteroid dehydrogenase (20±HSD) molecule from normal mature rat ovarian cytosol [Biochim. Biophys. Acta, 1991, 1079: 112-118]. In order to further characterize the 20±HSD and to obtain information for molecular cloning of the enzyme, we determined its N-terminal amino acid sequence. The sequence was shown to be Ser-Lys-lle-Gln-Lys-Met-Glu-Leu-Asn-Asp-Gly-His-Ser-lle-Pro-Val-Leu-Gly-Phe-Xaa-Thr. A search of the SWISS-PROT protein sequence database for N-terminal amino acid sequence similarities revealed 6 highly homologous proteins, including bovine prostaglandin F synthase, rat liver 3±hydroxysteroid dehydrogenase, bovine lens aldose reductase, human aldose reductase, frog 3±crystallin and human liver chlordecone reductase, suggesting that rat ovarian 20ar-HSD belongs to the aldo-keto reductase gene superfamily.

KW - 20α-Hydroxy steroid dehydrogenase

KW - Aldo-keto reductase

KW - Automatic Edman degradation

KW - N-terminal amino acid sequence

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Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily

Abstract

Keywords

ASJC Scopus subject areas

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