✦ LIBER ✦

Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase

✍ Scribed by Ramanath Majumdar; John R. Guest; William A. Bridger

Book ID: 113268427
Publisher: Elsevier Science
Year: 1991
Tongue: English
Weight: 386 KB
Volume: 1076
Category: Article
ISSN: 0167-4838
DOI: 10.1016/0167-4838(91)90223-m

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Probing the Nucleotide-Binding Site of E

Probing the Nucleotide-Binding Site of Escherichia coli Succinyl-CoA Synthetase †

✍ Joyce, Michael A.; Fraser, Marie E.; Brownie, Edward R.; James, Michael N. G.; B 📂 Article 📅 1999 🏛 American Chemical Society 🌐 English ⚖ 299 KB

Succinyl coenzyme A synthetase of Escher

Succinyl coenzyme A synthetase of Escherichia coli. Sequence of a peptide containing the active-site phosphohistidine residue

✍ Wang, T.; Jurasek, L.; Bridger, W. A. 📂 Article 📅 1972 🏛 American Chemical Society 🌐 English ⚖ 472 KB

Two Glutamate Residues, Glu 208α and Glu

Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase †

✍ Fraser, Marie E.; Joyce, Michael A.; Ryan, David G.; Wolodko, William T. 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 394 KB

Identification of tyrosine as a function

Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase

✍ Beata G. Vertessy; Petra Zalud; Per O. Nyman; Michael Zeppezauer 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 402 KB

Direct NMR resonance assignments of the

Direct NMR resonance assignments of the active site histidine residue in Escherichia coli thioesterase I/protease I/lysophospholipase L1

✍ Wen-Jin Wu; Sergiy I. Tyukhtenko; Tai-Huang Huang 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 156 KB

## Abstract Owing to the hydrogen‐bond interaction and rapid exchange rate with the bulk water, the transverse relaxation time for the N^δ1^H proton of the catalytic histidine in __Escherichia coli__ thioesterase I/protease I/lysophospholipase L~1~ (TEP‐I) is rather short. Because of its catalytic

Involvement of the carboxy-terminal resi

Involvement of the carboxy-terminal residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli

✍ Anderson, J. William; Bhanot, Pradeep; Georges, Fawzey; Klevit, Rachel E.; Waygo 📂 Article 📅 1991 🏛 American Chemical Society 🌐 English ⚖ 884 KB