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221 related items for PubMed ID: 17894825
1. High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli. Zocher G, Wiesand U, Schulz GE. FEBS J; 2007 Oct; 274(20):5382-9. PubMed ID: 17894825 [Abstract] [Full Text] [Related]
2. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF. Biochemistry; 2007 Jul 17; 46(28):8315-30. PubMed ID: 17583914 [Abstract] [Full Text] [Related]
3. Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli. Claus MT, Zocher GE, Maier TH, Schulz GE. Biochemistry; 2005 Jun 21; 44(24):8620-6. PubMed ID: 15952768 [Abstract] [Full Text] [Related]
4. Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound. Burkhard P, Tai CH, Jansonius JN, Cook PF. J Mol Biol; 2000 Oct 20; 303(2):279-86. PubMed ID: 11023792 [Abstract] [Full Text] [Related]
5. Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution. Oda Y, Mino K, Ishikawa K, Ataka M. J Mol Biol; 2005 Aug 12; 351(2):334-44. PubMed ID: 16005886 [Abstract] [Full Text] [Related]
6. Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN. J Mol Biol; 1999 Aug 27; 291(4):941-53. PubMed ID: 10452898 [Abstract] [Full Text] [Related]
7. Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN. J Mol Biol; 1998 Aug 27; 283(1):121-33. PubMed ID: 9761678 [Abstract] [Full Text] [Related]
13. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Rege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF. Biochemistry; 1996 Oct 15; 35(41):13485-93. PubMed ID: 8873618 [Abstract] [Full Text] [Related]
15. Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. Jäger J, Moser M, Sauder U, Jansonius JN. J Mol Biol; 1994 Jun 03; 239(2):285-305. PubMed ID: 8196059 [Abstract] [Full Text] [Related]
17. Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. Koellner G, Bzowska A, Wielgus-Kutrowska B, Luić M, Steiner T, Saenger W, Stepiński J. J Mol Biol; 2002 Jan 18; 315(3):351-71. PubMed ID: 11786017 [Abstract] [Full Text] [Related]