✦ LIBER ✦

Structural Determinants of Enzyme Binding Affinity: The E1 Component of Pyruvate Dehydrogenase from Escherichia coli in Complex with the Inhibitor Thiamin Thiazolone Diphosphate †,‡

✍ Scribed by Arjunan, Palaniappa; Chandrasekhar, Krishnamoorthy; Sax, Martin; Brunskill, Andrew; Nemeria, Natalia; Jordan, Frank; Furey, William

Book ID: 126999169
Publisher: American Chemical Society
Year: 2004
Tongue: English
Weight: 266 KB
Volume: 43
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi030200y

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Structure of the Pyruvate Dehydrogenase

Structure of the Pyruvate Dehydrogenase Multienzyme Complex E1 Component from Escherichia coli at 1.85 Å Resolution †,‡

✍ Arjunan, Palaniappa; Nemeria, Natalia; Brunskill, Andrew; Chandrasekhar, Krishna 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 698 KB

Active-site changes in the pyruvate dehy

Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 Å resolution

✍ Chandrasekhar, Krishnamoorthy ;Arjunan, Palaniappa ;Sax, Martin ;Nemeria, Natali 📂 Article 📅 2006 🏛 International Union of Crystallography 🌐 English ⚖ 587 KB

The first enzymatic component, E1 (EC 1.2.4.1), of the pyruvate dehydrogenase multienzyme complex (PDHc) utilizes thiamine diphosphate (ThDP) and Mg(2+) as cofactors. The structure of a branched-chain-specific E1 apoenzyme from the heterotetrameric alpha(2)beta(2) E1 family was recently reported and