✦ LIBER ✦

Catalytic Versatility, Stability, and Evolution of the (βα)8-Barrel Enzyme-Fold

✍ Scribed by Reinhard Sterner; Birte Hoecker

Publisher: John Wiley and Sons
Year: 2006
Weight: 9 KB
Volume: 37
Category: Article
ISSN: 0931-7597
DOI: 10.1002/chin.200607280

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Retracing Enzyme Evolution in the (βα)8-

Retracing Enzyme Evolution in the (βα)8-Barrel Scaffold

✍ James D. Stevenson; Stefan Lutz; Stephen J. Benkovic 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 87 KB

Related (βα)8-Barrel Proteins in Histidi

✍ Dr. Felix List; Prof. Dr. Reinhard Sterner; Dr. Matthias Wilmanns 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 974 KB

ChemInform Abstract: The Folding, Stabil

ChemInform Abstract: The Folding, Stability and Conformational Dynamics of β-Barrel Fluorescent Proteins

✍ Shang-Te Danny Hsu; Georg Blaser; Sophie E. Jackson 📂 Article 📅 2009 🏛 John Wiley and Sons ⚖ 12 KB

ChemInform Abstract: Related (βα)8-Barre

ChemInform Abstract: Related (βα)8-Barrel Proteins in Histidine and Tryptophan Biosynthesis: A Paradigm to Study Enzyme Evolution

✍ Felix List; Reinhard Sterner; Matthias Wilmanns 📂 Article 📅 2011 🏛 John Wiley and Sons ⚖ 20 KB

## Abstract Review: 49 refs.

α-Imino Esters: Versatile Substrates for

α-Imino Esters: Versatile Substrates for the Catalytic, Asymmetric Synthesis of α- and β-Amino Acids and β-Lactams

✍ Andrew E. Taggi; Ahmed M. Hafez; Thomas Lectka 📂 Article 📅 2003 🏛 John Wiley and Sons ⚖ 60 KB 👁 1 views

## Abstract For Abstract see ChemInform Abstract in Full Text.

High resolution structure and sequence o

High resolution structure and sequence of T. aurantiacus Xylanase I: Implications for the evolution of thermostability in family 10 xylanases and enzymes with βα-barrel architecture

✍ L. Lo Leggio; S. Kalogiannis; M.K. Bhat; R.W. Pickersgill 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 469 KB 👁 1 views

Xylanase I is a thermostable xylanase from the fungus Thermoascus aurantiacus, which belongs to family 10 in the current classification of glycosyl hydrolases. We have determined the three-dimensional X-ray structure of this enzyme to near atomic resolution (1.14 A ˚) by molecular replacement, and t