𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

✍ Scribed by Arjunan, Palaniappa; Nemeria, Natalia; Brunskill, Andrew; Chandrasekhar, Krishnamoorthy; Sax, Martin; Yan, ; Jordan, Frank; Guest, John R.; Furey, William

Book ID
126130929
Publisher
American Chemical Society
Year
2002
Tongue
English
Weight
698 KB
Volume
41
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

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