3BPB

Crystal structure of the dimethylarginine dimethylaminohydrolase H162G adduct with S-methyl-L-thiocitrulline

3BPB の概要

• エントリーDOI: 10.2210/pdb3bpb/pdb
• 分子名称: dimethylarginine dimethylaminohydrolase, N~5~-[(E)-imino(methylsulfanyl)methyl]-L-ornithine (3 entities in total)
• 機能のキーワード: enzyme adduct, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57261.40

構造登録者

Monzingo, A.F.,Linsky, T.W.,Stone, E.M.,Fast, W.,Robertus, J.D. (登録日: 2007-12-18, 公開日: 2008-06-17, 最終更新日: 2024-10-30)

主引用文献

Linsky, T.W.,Monzingo, A.F.,Stone, E.M.,Robertus, J.D.,Fast, W.
Promiscuous partitioning of a covalent intermediate common in the pentein superfamily.
Chem.Biol., 15:467-475, 2008

PubMed Abstract: Many enzymes in the pentein superfamily use a transient covalent intermediate in their catalytic mechanisms. Here we trap and determine the structure of a stable covalent adduct that mimics this intermediate using a mutant dimethylarginine dimethylaminohydrolase and an alternative substrate. The interactions observed between the enzyme and trapped adduct suggest an altered angle of attack between the nucleophiles of the first and second half-reactions of normal catalysis. The stable covalent adduct is also capable of further reaction. Addition of imidazole rescues the original hydrolytic activity. Notably, addition of other amines instead yields substituted arginine products, which arise from partitioning of the intermediate into the evolutionarily related amidinotransferase reaction pathway. The enzyme provides both selectivity and catalysis for the amidinotransferase reaction, underscoring commonalities among the reaction pathways in this mechanistically diverse enzyme superfamily. The promiscuous partitioning of this intermediate may also help to illuminate the evolutionary history of these enzymes.

PubMed: 18482699
DOI: 10.1016/j.chembiol.2008.03.012

実験手法

X-RAY DIFFRACTION (2.81 Å)