cDNA Cloning, Expression, and Characterization of the Human Bifunctional ATP Sulfurylase/Adenosine 5′-Phosphosulfate Kinase Enzyme

Ken YANAGISAWA; Yoichi SAKAKIBARA; Masahito SUIKO; Yasunari TAKAMI; Tatsuo NAKAYAMA; Hiroshi NAKAJIMA; Katsuhiko TAKAYANAGI; Yasuhiro NATORI; Ming-Cheh LIU

doi:10.1271/bbb.62.1037

Biological Chemistry Short Communication

cDNA Cloning, Expression, and Characterization of the Human Bifunctional ATP Sulfurylase/Adenosine 5′-Phosphosulfate Kinase Enzyme

Ken YANAGISAWA, Yoichi SAKAKIBARA, Masahito SUIKO, Yasunari TAKAMI, Tatsuo NAKAYAMA, Hiroshi NAKAJIMA, Katsuhiko TAKAYANAGI, Yasuhiro NATORI, Ming-Cheh LIU

Author information

Ken YANAGISAWA
Department of Biochemistry, University of Texas Health Center
Yoichi SAKAKIBARA
Department of Biochemistry, University of Texas Health Center
Masahito SUIKO
Department of Biochemistry, University of Texas Health Center
Yasunari TAKAMI
Department of Biochemistry, Miyazaki Medical College
Tatsuo NAKAYAMA
Department of Biochemistry, Miyazaki Medical College
Hiroshi NAKAJIMA
Department of Biochemistry, Unitika R & D Center
Katsuhiko TAKAYANAGI
Department of Biochemistry, Unitika R & D Center
Yasuhiro NATORI
Research Institute, International Medical Center of Japan
Ming-Cheh LIU
Department of Biochemistry, University of Texas Health Center

Keywords: ATP sulfurylase, APS kinase, bifunctional enzyme

JOURNAL FREE ACCESS

1998 Volume 62 Issue 5 Pages 1037-1040

DOI https://doi.org/10.1271/bbb.62.1037

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Abstract

A cDNA encoding the human bifunctional ATP sulfurylase/adenosine 5′-phosphosulfate (APS) kinase was cloned and sequenced. The enzyme contains an APS kinase domain in its N-terminal portion and an ATP sulfurylase domain in its C-terminal portion. Recombinant full-length enzyme and its constituent APS kinase and ATP sulfurylase domains were individually expressed, purified, and shown to have their respective enzymatic activities.

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