148 related articles for article (PubMed ID: 3606622)
1. The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase.
Hart KW; Clarke AR; Wigley DB; Chia WN; Barstow DA; Atkinson T; Holbrook JJ
Biochem Biophys Res Commun; 1987 Jul; 146(1):346-53. PubMed ID: 3606622
[TBL] [Abstract][Full Text] [Related]
2. A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase.
Hart KW; Clarke AR; Wigley DB; Waldman AD; Chia WN; Barstow DA; Atkinson T; Jones JB; Holbrook JJ
Biochim Biophys Acta; 1987 Aug; 914(3):294-8. PubMed ID: 3113484
[TBL] [Abstract][Full Text] [Related]
3. A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure.
Clarke AR; Wigley DB; Barstow DA; Chia WN; Atkinson T; Holbrook JJ
Biochim Biophys Acta; 1987 May; 913(1):72-80. PubMed ID: 3580377
[TBL] [Abstract][Full Text] [Related]
4. On the effects of replacing the carboxylate-binding arginine-171 by hydrophobic tyrosine or tryptophan residues in the L-lactate dehydrogenase from Bacillus stearothermophilus.
Luyten MA; Gold M; Friesen JD; Jones JB
Biochemistry; 1989 Aug; 28(16):6605-10. PubMed ID: 2790015
[TBL] [Abstract][Full Text] [Related]
5. Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase.
Nobbs TJ; Cortés A; Gelpi JL; Holbrook JJ; Atkinson T; Scawen MD; Nicholls DJ
Biochem J; 1994 Jun; 300 ( Pt 2)(Pt 2):491-9. PubMed ID: 8002955
[TBL] [Abstract][Full Text] [Related]
6. Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis.
Clarke AR; Wigley DB; Chia WN; Barstow D; Atkinson T; Holbrook JJ
Nature; 1986 Dec 18-31; 324(6098):699-702. PubMed ID: 3796734
[TBL] [Abstract][Full Text] [Related]
7. Attempting to remove the substrate inhibition of L-lactate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis.
Binay B; Karagüler NG
Appl Biochem Biotechnol; 2007; 141(2-3):265-72. PubMed ID: 18025556
[TBL] [Abstract][Full Text] [Related]
8. Threonine 246 at the active site of the L-lactate dehydrogenase of Bacillus stearothermophilus is important for catalysis but not for substrate binding.
Sakowicz R; Kallwass HK; Parris W; Kay CM; Jones JB; Gold M
Biochemistry; 1993 Nov; 32(47):12730-5. PubMed ID: 8251493
[TBL] [Abstract][Full Text] [Related]
9. Stringency of substrate specificity of Escherichia coli malate dehydrogenase.
Boernke WE; Millard CS; Stevens PW; Kakar SN; Stevens FJ; Donnelly MI
Arch Biochem Biophys; 1995 Sep; 322(1):43-52. PubMed ID: 7574693
[TBL] [Abstract][Full Text] [Related]
10. An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.
Clarke AR; Wilks HM; Barstow DA; Atkinson T; Chia WN; Holbrook JJ
Biochemistry; 1988 Mar; 27(5):1617-22. PubMed ID: 3365414
[TBL] [Abstract][Full Text] [Related]
11. Involvement of conserved lysine 68 of Bacillus stearothermophilus leucine dehydrogenase in substrate binding.
Sekimoto T; Fukui T; Tanizawa K
J Biol Chem; 1994 Mar; 269(10):7262-6. PubMed ID: 8125938
[TBL] [Abstract][Full Text] [Related]
12. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.
Wilks HM; Hart KW; Feeney R; Dunn CR; Muirhead H; Chia WN; Barstow DA; Atkinson T; Clarke AR; Holbrook JJ
Science; 1988 Dec; 242(4885):1541-4. PubMed ID: 3201242
[TBL] [Abstract][Full Text] [Related]
13. THR246 mutations decrease substrate inhibition in lactate dehydrogenase.
Sakowicz R; Kallwass H; Parris W; Gold M; Jones JB
Biochem Biophys Res Commun; 1992 Feb; 182(3):1309-12. PubMed ID: 1540173
[TBL] [Abstract][Full Text] [Related]
14. On the effect on specificity of Thr246----Gly mutation in L-lactate dehydrogenase of Bacillus sterothermophilus.
Bur D; Clarke T; Friesen JD; Gold M; Hart KW; Holbrook JJ; Jones JB; Luyten MA; Wilks HM
Biochem Biophys Res Commun; 1989 May; 161(1):59-63. PubMed ID: 2499337
[TBL] [Abstract][Full Text] [Related]
15. Source of catalysis in the lactate dehydrogenase system. Ground-state interactions in the enzyme-substrate complex.
Deng H; Zheng J; Clarke A; Holbrook JJ; Callender R; Burgner JW
Biochemistry; 1994 Mar; 33(8):2297-305. PubMed ID: 8117687
[TBL] [Abstract][Full Text] [Related]
16. Active-Loop Dynamics within the Michaelis Complex of Lactate Dehydrogenase from Bacillus stearothermophilus.
Nie B; Lodewyks K; Deng H; Desamero RZ; Callender R
Biochemistry; 2016 Jul; 55(27):3803-14. PubMed ID: 27319381
[TBL] [Abstract][Full Text] [Related]
17. Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity.
Clarke AR; Smith CJ; Hart KW; Wilks HM; Chia WN; Lee TV; Birktoft JJ; Banaszak LJ; Barstow DA; Atkinson T
Biochem Biophys Res Commun; 1987 Oct; 148(1):15-23. PubMed ID: 3314868
[TBL] [Abstract][Full Text] [Related]
18. A double mutant of highly purified Geobacillus stearothermophilus lactate dehydrogenase recognises l-mandelic acid as a substrate.
Binay B; Sessions RB; Karagüler NG
Enzyme Microb Technol; 2013 May; 52(6-7):393-9. PubMed ID: 23608509
[TBL] [Abstract][Full Text] [Related]
19. Dissecting the contributions of a specific side-chain interaction to folding and catalysis of Bacillus stearothermophilus lactate dehydrogenase.
Nicholls DJ; Wood IS; Nobbs TJ; Clarke AR; Holbrook JJ; Atkinson T; Scawen MD
Eur J Biochem; 1993 Mar; 212(2):447-55. PubMed ID: 8444183
[TBL] [Abstract][Full Text] [Related]
20. A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme.
Feeney R; Clarke AR; Holbrook JJ
Biochem Biophys Res Commun; 1990 Jan; 166(2):667-72. PubMed ID: 2302233
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
