✦ LIBER ✦

Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism

✍ Scribed by S. Benini; W. Rypniewski; K. Wilson; S. Ciurli; S. Mangani

Book ID: 106233055
Publisher: John Wiley and Sons
Year: 2001
Tongue: English
Weight: 537 KB
Volume: 6
Category: Article
ISSN: 1432-1327
DOI: 10.1007/s007750100254

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Structural properties of the nickel ions

Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms

✍ Stefano Ciurli; Stefano Benini; Wojciech R. Rypniewski; Keith S. Wilson; Silvia 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 472 KB

relationships between the structural features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme. In addition, the recently determined structure of a complex between urease and a transition state analogue is discussed as it leads to a novel, t

Insights into the mechanisms of catalysi

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 Å

✍ Lei Jin; Boguslaw Stec; William N. Lipscomb; Evan R. Kantrowitz 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 529 KB

A high-resolution structure of Escherichia coli aspartate transcarbamoylase has been determined to 2.1 Å; resolution in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate (PALA). The structure was refined to a free R-factor of 23.4% and a working R-factor of 20.3%. The PALA molecule