The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis

Mack Sobhany, Yoshimitsu Kakuta, Nobuo Sugiura, Koji Kimata, Masahiko Negishi

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

Bifunctional chondroitin synthase K4CP catalyzes glucuronic acid and N-acetylgalactosamine transfer activities and polymerizes a chondroitin chain. Here we have determined that an N-terminal region (residues 58-134) coordinates two transfer reactions and enables K4CP to catalyze polymerization. When residues 58-107 are deleted, K4CP loses polymerase activity while retaining both transfer activities. Peptide 113DWPSDL118within this N-terminal region interacts with C-terminal peptide 677YTWEKI 682. The deletion of either sequence abolishes glucuronic acid but not N-acetylgalactosamine transfer activity in K4CP. Both donor bindings and transfer activities are lost by mutating 677YTWEKI682 to 677DAWEDI682. On the other hand, acceptor substrates retain their binding to K4CP mutants. The characteristics of these K4CP mutants highlight different states of the enzyme reaction, providing an underlying structural basis for how these peptides play essential roles in coordinating the two glycosyltransferase activities for K4CP to elongate the chondroitin chain.

元の言語英語
ページ(範囲)36022-36028
ページ数7
ジャーナルJournal of Biological Chemistry
287
発行部数43
DOI
出版物ステータス出版済み - 10 19 2012

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Chondroitin
Glycosyltransferases
Biosynthesis
Acetylgalactosamine
Glucuronic Acid
Peptides
Sequence Deletion
Polymerization
Substrates
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Molecular Biology

これを引用

The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis. / Sobhany, Mack; Kakuta, Yoshimitsu; Sugiura, Nobuo; Kimata, Koji; Negishi, Masahiko.

:: Journal of Biological Chemistry, 巻 287, 番号 43, 19.10.2012, p. 36022-36028.

研究成果: ジャーナルへの寄稿記事

Sobhany, Mack ; Kakuta, Yoshimitsu ; Sugiura, Nobuo ; Kimata, Koji ; Negishi, Masahiko. / The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis. :: Journal of Biological Chemistry. 2012 ; 巻 287, 番号 43. pp. 36022-36028.
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abstract = "Bifunctional chondroitin synthase K4CP catalyzes glucuronic acid and N-acetylgalactosamine transfer activities and polymerizes a chondroitin chain. Here we have determined that an N-terminal region (residues 58-134) coordinates two transfer reactions and enables K4CP to catalyze polymerization. When residues 58-107 are deleted, K4CP loses polymerase activity while retaining both transfer activities. Peptide 113DWPSDL118within this N-terminal region interacts with C-terminal peptide 677YTWEKI 682. The deletion of either sequence abolishes glucuronic acid but not N-acetylgalactosamine transfer activity in K4CP. Both donor bindings and transfer activities are lost by mutating 677YTWEKI682 to 677DAWEDI682. On the other hand, acceptor substrates retain their binding to K4CP mutants. The characteristics of these K4CP mutants highlight different states of the enzyme reaction, providing an underlying structural basis for how these peptides play essential roles in coordinating the two glycosyltransferase activities for K4CP to elongate the chondroitin chain.",
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AU - Negishi, Masahiko

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N2 - Bifunctional chondroitin synthase K4CP catalyzes glucuronic acid and N-acetylgalactosamine transfer activities and polymerizes a chondroitin chain. Here we have determined that an N-terminal region (residues 58-134) coordinates two transfer reactions and enables K4CP to catalyze polymerization. When residues 58-107 are deleted, K4CP loses polymerase activity while retaining both transfer activities. Peptide 113DWPSDL118within this N-terminal region interacts with C-terminal peptide 677YTWEKI 682. The deletion of either sequence abolishes glucuronic acid but not N-acetylgalactosamine transfer activity in K4CP. Both donor bindings and transfer activities are lost by mutating 677YTWEKI682 to 677DAWEDI682. On the other hand, acceptor substrates retain their binding to K4CP mutants. The characteristics of these K4CP mutants highlight different states of the enzyme reaction, providing an underlying structural basis for how these peptides play essential roles in coordinating the two glycosyltransferase activities for K4CP to elongate the chondroitin chain.

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