4ISS

SeMet-substituted Kluyveromyces lactis Allophanate Hydrolase

4ISS の概要

• エントリーDOI: 10.2210/pdb4iss/pdb
• 関連するPDBエントリー: 4IST
• 分子名称: Allophanate Hydrolase, D(-)-TARTARIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: mixed alpha and beta structure, allophanate binding, hydrolase
• 由来する生物種: Kluyveromyces lactis (Yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141921.92

構造登録者

Fan, C.,Xiang, S. (登録日: 2013-01-17, 公開日: 2013-06-19, 最終更新日: 2024-11-20)

主引用文献

Fan, C.,Li, Z.,Yin, H.,Xiang, S.
Structure and function of allophanate hydrolase.
J.Biol.Chem., 288:21422-21432, 2013

PubMed Abstract: Allophanate hydrolase converts allophanate to ammonium and carbon dioxide. It is conserved in many organisms and is essential for their utilization of urea as a nitrogen source. It also has important functions in a newly discovered eukaryotic pyrimidine nucleic acid precursor degradation pathway, the yeast-hypha transition that several pathogens utilize to escape the host defense, and an s-triazine herbicide degradation pathway recently emerged in many soil bacteria. We have determined the crystal structure of the Kluyveromyces lactis allophanate hydrolase. Together with structure-directed functional studies, we demonstrate that its N and C domains catalyze a two-step reaction and contribute to maintaining a dimeric form of the enzyme required for their optimal activities. Our studies also provide molecular insights into their catalytic mechanism. Interestingly, we found that the C domain probably catalyzes a novel form of decarboxylation reaction that might expand the knowledge of this common reaction in biological systems.

PubMed: 23754281
DOI: 10.1074/jbc.M113.453837

実験手法

X-RAY DIFFRACTION (2.5 Å)