145 related articles for article (PubMed ID: 7696265)
1. Use of site-directed mutagenesis and alternative substrates to assign the prototropic groups important to catalysis by Escherichia coli aspartate aminotransferase.
Gloss LM; Kirsch JF
Biochemistry; 1995 Mar; 34(12):3999-4007. PubMed ID: 7696265
[TBL] [Abstract][Full Text] [Related]
2. Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine.
Gloss LM; Kirsch JF
Biochemistry; 1995 Mar; 34(12):3990-8. PubMed ID: 7696264
[TBL] [Abstract][Full Text] [Related]
3. The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis.
Goldberg JM; Kirsch JF
Biochemistry; 1996 Apr; 35(16):5280-91. PubMed ID: 8611515
[TBL] [Abstract][Full Text] [Related]
4. The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.
Goldberg JM; Swanson RV; Goodman HS; Kirsch JF
Biochemistry; 1991 Jan; 30(1):305-12. PubMed ID: 1988027
[TBL] [Abstract][Full Text] [Related]
5. Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift.
Toney MD; Kirsch JF
Biochemistry; 1993 Feb; 32(6):1471-9. PubMed ID: 8431426
[TBL] [Abstract][Full Text] [Related]
6. Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
Gloss LM; Kirsch JF
Biochemistry; 1995 Sep; 34(38):12323-32. PubMed ID: 7547975
[TBL] [Abstract][Full Text] [Related]
7. Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.
Park Y; Luo J; Schultz PG; Kirsch JF
Biochemistry; 1997 Aug; 36(34):10517-25. PubMed ID: 9265632
[TBL] [Abstract][Full Text] [Related]
8. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Yano T; Kuramitsu S; Tanase S; Morino Y; Kagamiyama H
Biochemistry; 1992 Jun; 31(25):5878-87. PubMed ID: 1610831
[TBL] [Abstract][Full Text] [Related]
9. Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine.
Planas A; Kirsch JF
Biochemistry; 1991 Aug; 30(33):8268-76. PubMed ID: 1907854
[TBL] [Abstract][Full Text] [Related]
10. Shift in pH-rate profile and enhanced discrimination between dicarboxylic and aromatic substrates in mitochondrial aspartate aminotransferase Y70H.
Pan P; Jaussi R; Gehring H; Giannattasio S; Christen P
Biochemistry; 1994 Mar; 33(10):2757-60. PubMed ID: 8130187
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase.
Shaffer WA; Luong TN; Rothman SC; Kirsch JF
Protein Sci; 2002 Dec; 11(12):2848-59. PubMed ID: 12441383
[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. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
Jeffery CJ; Gloss LM; Petsko GA; Ringe D
Protein Eng; 2000 Feb; 13(2):105-12. PubMed ID: 10708649
[TBL] [Abstract][Full Text] [Related]
15. Irreversible inactivation of aspartate aminotransferase by 2-oxoglutaconic acid and its dimethyl ester.
Kato Y; Asano Y; Makar TK; Cooper AJ
J Biochem; 1996 Sep; 120(3):531-9. PubMed ID: 8902617
[TBL] [Abstract][Full Text] [Related]
16. Contribution to catalysis and stability of the five cysteines in Escherichia coli aspartate aminotransferase. Preparation and properties of a cysteine-free enzyme.
Gloss LM; Planas A; Kirsch JF
Biochemistry; 1992 Jan; 31(1):32-9. PubMed ID: 1731883
[TBL] [Abstract][Full Text] [Related]
17. Mutational, kinetic, and NMR studies of the mechanism of E. coli GDP-mannose mannosyl hydrolase, an unusual Nudix enzyme.
Legler PM; Massiah MA; Mildvan AS
Biochemistry; 2002 Sep; 41(35):10834-48. PubMed ID: 12196023
[TBL] [Abstract][Full Text] [Related]
18. A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase.
Yano T; Mizuno T; Kagamiyama H
Biochemistry; 1993 Feb; 32(7):1810-5. PubMed ID: 8439541
[TBL] [Abstract][Full Text] [Related]
19. Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.
Vacca RA; Giannattasio S; Graber R; Sandmeier E; Marra E; Christen P
J Biol Chem; 1997 Aug; 272(35):21932-7. PubMed ID: 9268327
[TBL] [Abstract][Full Text] [Related]
20. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.
Schafer SL; Barrett WC; Kallarakal AT; Mitra B; Kozarich JW; Gerlt JA; Clifton JG; Petsko GA; Kenyon GL
Biochemistry; 1996 May; 35(18):5662-9. PubMed ID: 8639525
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
