1ERZ
CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES
1ERZ の概要
| エントリーDOI | 10.2210/pdb1erz/pdb |
| 分子名称 | N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE (2 entities in total) |
| 機能のキーワード | four-layer sandwich, hydrolase |
| 由来する生物種 | Agrobacterium sp. |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 68398.19 |
| 構造登録者 | Nakai, T.,Hasegawa, T.,Yamashita, E.,Yamamoto, M.,Kumasaka, T.,Ueki, T.,Nanba, H.,Ikenaka, Y.,Takahashi, S.,Sato, M.,Tsukihara, T. (登録日: 2000-04-06, 公開日: 2001-04-06, 最終更新日: 2024-02-07) |
| 主引用文献 | Nakai, T.,Hasegawa, T.,Yamashita, E.,Yamamoto, M.,Kumasaka, T.,Ueki, T.,Nanba, H.,Ikenaka, Y.,Takahashi, S.,Sato, M.,Tsukihara, T. Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases. Structure Fold.Des., 8:729-737, 2000 Cited by PubMed Abstract: N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we have determined the structure of DCase from Agrobacterium sp. strain KNK712. PubMed: 10903946DOI: 10.1016/S0969-2126(00)00160-X 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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