FUGUEによる微生物ゲノム由来仮説蛋白質のアノテーション

• 白井 宏樹

  ケンブリッジ大・生化学

• Tom Blundell

  ケンブリッジ大・生化学

• 水口 賢司

  ケンブリッジ大・生化学

書誌事項

タイトル別名

• FUGUE annotated hypothetical proteins derived from microbial genomes

抄録

Thre enzymes to catalyze the modification of arginine, peptidyl-arginine deiminase (PAD; EC 3.5.3.15) from Porphyromonas gingivalis, arginine deiminase (ADI; EC 3.5.3.6), and amidinotransferase (AT; EC 2.1.4) are traditionally classified separately. Only AT has been determined its structure by experiment. Although both PAD and ADI are attractive drug targets, attempts to design inhibitor have been hampered due to the lack of knowledge of their catalytic mechanism. By combining PSI-BLAST and FUGUE, we show in this report that these enzymes belong to a novel superfamily sharing similar catalytic mechanisms. FUGUE is our sequence-structure homology recognition program whose performance has been extensively benchmarked (see, e.g., http://cafasp.bioinfo.pl). After PAD from Porphyromonas gingivalis and ADI were predicted to be evolutionary related to AT by PSI-BLAST and FUGUE, we verified these identification by the conservation of structurally or functionally important residues. Based on the catalytic mechanism of AT, we could propose catalytic mechanisms of ADI and PAD. They should be helpful in designing inhibitors for these potential drug targets.

収録刊行物

• 情報化学討論会・構造活性相関シンポジウム講演要旨集

  情報化学討論会・構造活性相関シンポジウム講演要旨集 tokusi (0), K17-K17, 2001

  日本化学会情報化学部会・日本薬学会構造活性相関部会

キーワード

• バイオインフォーマティクス
• アノテーション
• ゲノム創薬

詳細情報

• CRID: 1390282680569289856
• NII論文ID: 130004575402
• DOI: 10.11547/ciqs2001.tokusi.0.k17.0
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可