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Items: 1 to 20 of 187

1.

Virtual screening of mandelate racemase mutants with enhanced activity based on binding energy in the transition state.

Gu J, Liu M, Guo F, Xie W, Lu W, Ye L, Chen Z, Yuan S, Yu H.

Enzyme Microb Technol. 2014 Feb 5;55:121-7. doi: 10.1016/j.enzmictec.2013.10.008. Epub 2013 Nov 1.

PMID:
24411454
2.

Mutational analysis of the active site flap (20s loop) of mandelate racemase.

Bourque JR, Bearne SL.

Biochemistry. 2008 Jan 15;47(2):566-78. Epub 2007 Dec 20.

PMID:
18092808
3.

Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis.

Siddiqi F, Bourque JR, Jiang H, Gardner M, St Maurice M, Blouin C, Bearne SL.

Biochemistry. 2005 Jun 28;44(25):9013-21.

PMID:
15966725
4.
5.

Hydrophobic nature of the active site of mandelate racemase.

St Maurice M, Bearne SL.

Biochemistry. 2004 Mar 9;43(9):2524-32.

PMID:
14992589
6.

Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.

Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL.

Biochemistry. 1995 Mar 7;34(9):2788-97.

PMID:
7893690
7.

The role of residue S139 of mandelate racemase: synergistic effect of S139 and E317 on transition state stabilization.

Gu J, Yu H.

J Biomol Struct Dyn. 2012;30(5):585-93. doi: 10.1080/07391102.2012.687524. Epub 2012 Jun 26.

PMID:
22731931
9.

Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.

Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL.

Biochemistry. 1995 Mar 7;34(9):2777-87.

PMID:
7893689
10.

Directed evolution of mandelate racemase by a novel high-throughput screening method.

Yang C, Ye L, Gu J, Yang X, Li A, Yu H.

Appl Microbiol Biotechnol. 2017 Feb;101(3):1063-1072. doi: 10.1007/s00253-016-7790-3. Epub 2016 Aug 24.

PMID:
27557723
11.

An additional role for the Brønsted acid-base catalysts of mandelate racemase in transition state stabilization.

Nagar M, Bearne SL.

Biochemistry. 2015 Nov 10;54(44):6743-52. doi: 10.1021/acs.biochem.5b00982. Epub 2015 Nov 2.

PMID:
26480244
12.

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 7;35(18):5662-9.

PMID:
8639525
13.

Structure of mandelate racemase with bound intermediate analogues benzohydroxamate and cupferron.

Lietzan AD, Nagar M, Pellmann EA, Bourque JR, Bearne SL, St Maurice M.

Biochemistry. 2012 Feb 14;51(6):1160-70. doi: 10.1021/bi2018514. Epub 2012 Feb 3.

14.

Using directed evolution to probe the substrate specificity of mandelamide hydrolase.

Wang PF, Yep A, Kenyon GL, McLeish MJ.

Protein Eng Des Sel. 2009 Feb;22(2):103-10. doi: 10.1093/protein/gzn073. Epub 2008 Dec 10.

PMID:
19074156
15.

Redefining the minimal substrate tolerance of mandelate racemase. Racemization of trifluorolactate.

Nagar M, Narmandakh A, Khalak Y, Bearne SL.

Biochemistry. 2011 Oct 18;50(41):8846-52. doi: 10.1021/bi201188j. Epub 2011 Sep 21.

PMID:
21894901
16.
17.

A QM/MM study of the racemization of vinylglycolate catalyzed by mandelate racemase enzyme.

Garcia-Viloca M, González-Lafont A, Lluch JM.

J Am Chem Soc. 2001 Jan 31;123(4):709-21.

PMID:
11456585
18.

Potent inhibition of mandelate racemase by a fluorinated substrate-product analogue with a novel binding mode.

Nagar M, Lietzan AD, St Maurice M, Bearne SL.

Biochemistry. 2014 Feb 25;53(7):1169-78. doi: 10.1021/bi401703h. Epub 2014 Feb 10.

PMID:
24472022
19.

Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position 84 as a hot spot for β-elimination function.

Nelson DL, Applegate GA, Beio ML, Graham DL, Berkowitz DB.

J Biol Chem. 2017 Aug 25;292(34):13986-14002. doi: 10.1074/jbc.M117.777904. Epub 2017 Jul 10.

PMID:
28696262
20.

Restructuring catalysis in the mandelate pathway.

Neidhart DC, Howell PL, Petsko GA, Gerlt JA, Kozarich JW, Powers VM, Kenyon GL.

Biochem Soc Symp. 1990;57:135-41.

PMID:
2099737

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