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Journal Abstract Search

158 related items for PubMed ID: 9933615

  • 1. Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5'-phosphate. Chemical rescue studies of Lys39 --> Ala mutant.
    Watanabe A, Kurokawa Y, Yoshimura T, Kurihara T, Soda K, Esaki N.
    J Biol Chem; 1999 Feb 12; 274(7):4189-94. PubMed ID: 9933615
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  • 2. Transamination as a side-reaction catalyzed by alanine racemase of Bacillus stearothermophilus.
    Kurokawa Y, Watanabe A, Yoshimura T, Esaki N, Soda K.
    J Biochem; 1998 Dec 01; 124(6):1163-9. PubMed ID: 9832621
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  • 3. Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine.
    Watanabe A, Yoshimura T, Mikami B, Esaki N.
    J Biochem; 1999 Oct 01; 126(4):781-6. PubMed ID: 10502689
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  • 4. Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine.
    Watanabe A, Yoshimura T, Mikami B, Hayashi H, Kagamiyama H, Esaki N.
    J Biol Chem; 2002 May 24; 277(21):19166-72. PubMed ID: 11886871
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  • 6. Understanding catalytic specificity in alanine racemase from quantum mechanical and molecular mechanical simulations of the arginine 219 mutant.
    Rubinstein A, Major DT.
    Biochemistry; 2010 May 11; 49(18):3957-64. PubMed ID: 20394349
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  • 7. Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate.
    Yoshimura T, Bhatia MB, Manning JM, Ringe D, Soda K.
    Biochemistry; 1992 Dec 01; 31(47):11748-54. PubMed ID: 1445909
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  • 8. Racemization of alanine by the alanine racemases from Salmonella typhimurium and Bacillus stearothermophilus: energetic reaction profiles.
    Faraci WS, Walsh CT.
    Biochemistry; 1988 May 03; 27(9):3267-76. PubMed ID: 3291946
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  • 9. Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase.
    Sun S, Toney MD.
    Biochemistry; 1999 Mar 30; 38(13):4058-65. PubMed ID: 10194319
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  • 10. Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.
    Morollo AA, Petsko GA, Ringe D.
    Biochemistry; 1999 Mar 16; 38(11):3293-301. PubMed ID: 10079072
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  • 11. Conversion of a PLP-dependent racemase into an aldolase by a single active site mutation.
    Seebeck FP, Hilvert D.
    J Am Chem Soc; 2003 Aug 27; 125(34):10158-9. PubMed ID: 12926923
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  • 12. Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine racemase.
    Spies MA, Toney MD.
    Biochemistry; 2003 May 06; 42(17):5099-107. PubMed ID: 12718553
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  • 13. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.
    Shaw JP, Petsko GA, Ringe D.
    Biochemistry; 1997 Feb 11; 36(6):1329-42. PubMed ID: 9063881
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  • 15. Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies.
    Bhavani S, Trivedi V, Jala VR, Subramanya HS, Kaul P, Prakash V, Appaji Rao N, Savithri HS.
    Biochemistry; 2005 May 10; 44(18):6929-37. PubMed ID: 15865438
    [Abstract] [Full Text] [Related]

  • 16. Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine.
    Nishimura K, Tanizawa K, Yoshimura T, Esaki N, Futaki S, Manning JM, Soda K.
    Biochemistry; 1991 Apr 23; 30(16):4072-7. PubMed ID: 1902115
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  • 17. Thermostable alanine racemase of Bacillus stearothermophilus: subunit dissociation and unfolding.
    Toyama H, Esaki N, Yoshimura T, Tanizawa K, Soda K.
    J Biochem; 1991 Aug 23; 110(2):279-83. PubMed ID: 1761523
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