✦ LIBER ✦

Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site

✍ Scribed by Der-Ing Liao; Edith C Wolff; Myung Hee Park; David R Davies

Book ID: 114329552
Publisher: Elsevier Science
Year: 1998
Tongue: English
Weight: 1014 KB
Volume: 6
Category: Article
ISSN: 0969-2126
DOI: 10.1016/s0969-2126(98)00004-5

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Crystal Structure of Human E1 Enzyme and

Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase Activity

✍ Hui Wang; Hai Pang; Mark Bartlam; Zihe Rao 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 442 KB

Crystal Structure of Human Arylsulfatase

Crystal Structure of Human Arylsulfatase A: The Aldehyde Function and the Metal Ion at the Active Site Suggest a Novel Mechanism for Sulfate Ester Hydrolysis †,‡

✍ Lukatela, G.; Krauss, N.; Theis, K.; Selmer, T.; Gieselmann, V.; von Figura, K.; 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 275 KB

Crystal Structures of Adrenodoxin Reduct

Crystal Structures of Adrenodoxin Reductase in Complex with NADP + and NADPH Suggesting a Mechanism for the Electron Transfer of an Enzyme Family †,‡

✍ Ziegler, Gabriele A.; Schulz, Georg E. 📂 Article 📅 2000 🏛 American Chemical Society 🌐 English ⚖ 673 KB

Crystal structures of two human pyrophos

Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture

✍ Peneff, C. 📂 Article 📅 2001 🏛 Nature Publishing Group 🌐 English ⚖ 616 KB

Models for the Active Center of Pterin-C

Models for the Active Center of Pterin-Containing Molybdenum Enzymes: Crystal structure of a molybdenum complex with sulfur and pterin ligands

✍ Berthold Fischer; Helmut W. Schmalle; Markus R. Baumgartner; Max Viscontini 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 German ⚖ 485 KB 👁 1 views

2-amino-5,6,7,8-tetrahydropteridin-4(3H)-one.

Exploring the chiral space within the ac

Exploring the chiral space within the active site of α-thrombin with a constrained mimic of d-Phe-Pro-Arg — design, synthesis, inhibitory activity, and X-ray structure of an enzyme–inhibitor complex

✍ Stephen Hanessian; Elise Balaux; Djorde Musil; Lise-Lotte Olsson; Ingemar Nilsso 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 356 KB

An indolizidinone motif with strategically placed substitutents was designed and synthesized as a constrained mimic of D-Phe-Pro-Arg. Low nanomolar inhibition of alpha-thrombin validates the design elements in this inhibitor which also exhibits a 20-fold selectivity for thrombin versus trypsin. An X