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481 related items for PubMed ID: 15938611
1. Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step. Islam MM, Goto M, Miyahara I, Ikushiro H, Hirotsu K, Hayashi H. Biochemistry; 2005 Jun 14; 44(23):8218-29. PubMed ID: 15938611 [Abstract] [Full Text] [Related]
2. The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis. Hayashi H, Mizuguchi H, Kagamiyama H. Biochemistry; 1998 Oct 27; 37(43):15076-85. PubMed ID: 9790670 [Abstract] [Full Text] [Related]
4. Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate. Hester G, Stark W, Moser M, Kallen J, Marković-Housley Z, Jansonius JN. J Mol Biol; 1999 Feb 26; 286(3):829-50. PubMed ID: 10024454 [Abstract] [Full Text] [Related]
5. 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]
6. Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme. Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu K. Biochemistry; 2003 Apr 08; 42(13):3725-33. PubMed ID: 12667063 [Abstract] [Full Text] [Related]
7. Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. Storici P, Capitani G, Müller R, Schirmer T, Jansonius JN. J Mol Biol; 1999 Jan 08; 285(1):297-309. PubMed ID: 9878407 [Abstract] [Full Text] [Related]
8. Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Malashkevich VN, Toney MD, Jansonius JN. Biochemistry; 1993 Dec 14; 32(49):13451-62. PubMed ID: 7903048 [Abstract] [Full Text] [Related]
9. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A. J Mol Biol; 2001 Aug 24; 311(4):761-76. PubMed ID: 11518529 [Abstract] [Full Text] [Related]
10. Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase. Toney MD, Hohenester E, Keller JW, Jansonius JN. J Mol Biol; 1995 Jan 13; 245(2):151-79. PubMed ID: 7799433 [Abstract] [Full Text] [Related]
11. Mechanism of substrate recognition and PLP-induced conformational changes in LL-diaminopimelate aminotransferase from Arabidopsis thaliana. Watanabe N, Clay MD, van Belkum MJ, Cherney MM, Vederas JC, James MN. J Mol Biol; 2008 Dec 31; 384(5):1314-29. PubMed ID: 18952095 [Abstract] [Full Text] [Related]
12. Transient-state kinetics of the reaction of aspartate aminotransferase with aspartate at low pH reveals dual routes in the enzyme-substrate association process. Hayashi H, Kagamiyama H. Biochemistry; 1997 Nov 04; 36(44):13558-69. PubMed ID: 9354624 [Abstract] [Full Text] [Related]
13. Aromatic L-amino acid decarboxylase: conformational change in the flexible region around Arg334 is required during the transaldimination process. Ishii S, Hayashi H, Okamoto A, Kagamiyama H. Protein Sci; 1998 Aug 04; 7(8):1802-10. PubMed ID: 10082378 [Abstract] [Full Text] [Related]
14. Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. Park Y, Luo J, Schultz PG, Kirsch JF. Biochemistry; 1997 Aug 26; 36(34):10517-25. PubMed ID: 9265632 [Abstract] [Full Text] [Related]
15. Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H. J Biol Chem; 2003 Mar 14; 278(11):9481-8. PubMed ID: 12488449 [Abstract] [Full Text] [Related]
16. [Study of crystals of aspartate aminotransferase complexed with D-aspartate]. Kochkina VM, Korolev SV, Meador WE, Wilson D, Quiocho FA, Kuzin AP. Mol Biol (Mosk); 1994 Mar 14; 28(2):333-41. PubMed ID: 8183265 [Abstract] [Full Text] [Related]
17. Active site model for gamma-aminobutyrate aminotransferase explains substrate specificity and inhibitor reactivities. Toney MD, Pascarella S, De Biase D. Protein Sci; 1995 Nov 14; 4(11):2366-74. PubMed ID: 8563634 [Abstract] [Full Text] [Related]
18. Reaction of aspartate aminotransferase with C5-dicarboxylic acids: comparison with the reaction with C4-dicarboxylic acids. Islam MM, Hayashi H, Kagamiyama H. J Biochem; 2003 Aug 14; 134(2):277-85. PubMed ID: 12966078 [Abstract] [Full Text] [Related]
19. Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D. Biochemistry; 1998 Apr 07; 37(14):4958-67. PubMed ID: 9538014 [Abstract] [Full Text] [Related]
20. Structure and mechanism of a cysteine sulfinate desulfinase engineered on the aspartate aminotransferase scaffold. Fernandez FJ, de Vries D, Peña-Soler E, Coll M, Christen P, Gehring H, Vega MC. Biochim Biophys Acta; 2012 Feb 07; 1824(2):339-49. PubMed ID: 22138634 [Abstract] [Full Text] [Related] Page: [Next] [New Search]