Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

My NCBI Filters
Text availability
Article attribute
Article type
Publication date

Search Results

121 results
Filters applied: . Clear all Results are displayed in a computed author sort order. Results by year timeline is unavailable
Page 1
Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida.
Röther D, Poppe L, Viergutz S, Langer B, Rétey J. Röther D, et al. Among authors: retey j. Eur J Biochem. 2001 Dec;268(23):6011-9. doi: 10.1046/j.0014-2956.2001.02298.x. Eur J Biochem. 2001. PMID: 11732994
Elucidation of the 3D structure of histidine ammonia-lyase (HAL, EC 4.3.1.3) from Pseudomonas putida by X-ray crystallography revealed that the electrophilic prosthetic group at the active site is 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) [Schwede, T.F., Retey, …
Elucidation of the 3D structure of histidine ammonia-lyase (HAL, EC 4.3.1.3) from Pseudomonas putida by X-ray crystallography revealed that …
The behavior of substrate analogues and secondary deuterium isotope effects in the phenylalanine ammonia-lyase reaction.
Gloge A, Langer B, Poppe L, Rétey J. Gloge A, et al. Among authors: retey j. Arch Biochem Biophys. 1998 Nov 1;359(1):1-7. doi: 10.1006/abbi.1998.0860. Arch Biochem Biophys. 1998. PMID: 9799553
Metacresol and glycine can be thought as a dissection of metatyrosine, which is an excellent substrate of phenylalanine ammonia-lyase (PAL) (B. Schuster and J. Retey, PNAS 92, 8433, 1995). Whereas metacresol was a very weak inhibitor and glycine was inert, simultane …
Metacresol and glycine can be thought as a dissection of metatyrosine, which is an excellent substrate of phenylalanine ammonia-lyase (PAL) …
121 results