142 related articles for article (PubMed ID: 7664122)
1. Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Malashkevich VN; Onuffer JJ; Kirsch JF; Jansonius JN
Nat Struct Biol; 1995 Jul; 2(7):548-53. PubMed ID: 7664122
[TBL] [Abstract][Full Text] [Related]
2. Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
Onuffer JJ; Kirsch JF
Protein Sci; 1995 Sep; 4(9):1750-7. PubMed ID: 8528073
[TBL] [Abstract][Full Text] [Related]
3. Significant improvement to the catalytic properties of aspartate aminotransferase: role of hydrophobic and charged residues in the substrate binding pocket.
Köhler E; Seville M; Jäger J; Fotheringham I; Hunter M; Edwards M; Jansonius JN; Kirschner K
Biochemistry; 1994 Jan; 33(1):90-7. PubMed ID: 7904477
[TBL] [Abstract][Full Text] [Related]
4. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.
Onuffer JJ; Ton BT; Klement I; Kirsch JF
Protein Sci; 1995 Sep; 4(9):1743-9. PubMed ID: 8528072
[TBL] [Abstract][Full Text] [Related]
5. 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; 1824(2):339-49. PubMed ID: 22138634
[TBL] [Abstract][Full Text] [Related]
6. Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.
Rothman SC; Voorhies M; Kirsch JF
Protein Sci; 2004 Mar; 13(3):763-72. PubMed ID: 14767072
[TBL] [Abstract][Full Text] [Related]
7. Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.
Danishefsky AT; Onnufer JJ; Petsko GA; Ringe D
Biochemistry; 1991 Feb; 30(7):1980-5. PubMed ID: 1993208
[TBL] [Abstract][Full Text] [Related]
8. Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase.
Chow MA; McElroy KE; Corbett KD; Berger JM; Kirsch JF
Biochemistry; 2004 Oct; 43(40):12780-7. PubMed ID: 15461450
[TBL] [Abstract][Full Text] [Related]
9. Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.
Inoue K; Kuramitsu S; Okamoto A; Hirotsu K; Higuchi T; Morino Y; Kagamiyama H
J Biochem; 1991 Apr; 109(4):570-6. PubMed ID: 1869510
[TBL] [Abstract][Full Text] [Related]
10. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
Ko TP; Wu SP; Yang WZ; Tsai H; Yuan HS
Acta Crystallogr D Biol Crystallogr; 1999 Aug; 55(Pt 8):1474-7. PubMed ID: 10417420
[TBL] [Abstract][Full Text] [Related]
11. Three-dimensional structure of a mutant E. coli aspartate aminotransferase with increased enzymic activity.
Jäger J; Pauptit RA; Sauder U; Jansonius JN
Protein Eng; 1994 May; 7(5):605-12. PubMed ID: 8073030
[TBL] [Abstract][Full Text] [Related]
12. Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli.
Collier RH; Kohlhaw G
J Bacteriol; 1972 Oct; 112(1):365-71. PubMed ID: 4404056
[TBL] [Abstract][Full Text] [Related]
13. How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase.
Rothman SC; Kirsch JF
J Mol Biol; 2003 Mar; 327(3):593-608. PubMed ID: 12634055
[TBL] [Abstract][Full Text] [Related]
14. Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode.
Blankenfeldt W; Nowicki C; Montemartini-Kalisz M; Kalisz HM; Hecht HJ
Protein Sci; 1999 Nov; 8(11):2406-17. PubMed ID: 10595543
[TBL] [Abstract][Full Text] [Related]
15. Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1β aspartate aminotransferase.
Giustini C; Graindorge M; Cobessi D; Crouzy S; Robin A; Curien G; Matringe M
FEBS J; 2019 Jun; 286(11):2118-2134. PubMed ID: 30771275
[TBL] [Abstract][Full Text] [Related]
16. Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
Vacca RA; Christen P; Malashkevich VN; Jansonius JN; Sandmeier E
Eur J Biochem; 1995 Jan; 227(1-2):481-7. PubMed ID: 7851426
[TBL] [Abstract][Full Text] [Related]
17. Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme.
Graber R; Kasper P; Malashkevich VN; Sandmeier E; Berger P; Gehring H; Jansonius JN; Christen P
Eur J Biochem; 1995 Sep; 232(2):686-90. PubMed ID: 7556224
[TBL] [Abstract][Full Text] [Related]
18. [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.
Hayashi H; Kuramitsu S; Inoue Y; Morino Y; Kagamiyama H
Biochem Biophys Res Commun; 1989 Feb; 159(1):337-42. PubMed ID: 2564274
[TBL] [Abstract][Full Text] [Related]
19. Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.
Inoue K; Kuramitsu S; Okamoto A; Hirotsu K; Higuchi T; Kagamiyama H
Biochemistry; 1991 Aug; 30(31):7796-801. PubMed ID: 1868057
[TBL] [Abstract][Full Text] [Related]
20. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Almo SC; Smith DL; Danishefsky AT; Ringe D
Protein Eng; 1994 Mar; 7(3):405-12. PubMed ID: 7909946
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]