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Items: 1 to 20 of 115

1.

A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase.

Basran J, Rafice SA, Chauhan N, Efimov I, Cheesman MR, Ghamsari L, Raven EL.

Biochemistry. 2008 Apr 22;47(16):4752-60. doi: 10.1021/bi702393b. Epub 2008 Mar 28.

PMID:
18370401
2.

The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.

Chauhan N, Basran J, Efimov I, Svistunenko DA, Seward HE, Moody PC, Raven EL.

Biochemistry. 2008 Apr 22;47(16):4761-9. doi: 10.1021/bi702405a. Epub 2008 Mar 28.

PMID:
18370410
3.

Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.

Rafice SA, Chauhan N, Efimov I, Basran J, Raven EL.

Biochem Soc Trans. 2009 Apr;37(Pt 2):408-12. doi: 10.1042/BST0370408. Review.

PMID:
19290871
4.

Initial O₂ Insertion Step of the Tryptophan Dioxygenase Reaction Proposed by a Heme-Modification Study.

Makino R, Obayashi E, Hori H, Iizuka T, Mashima K, Shiro Y, Ishimura Y.

Biochemistry. 2015 Jun 16;54(23):3604-16. doi: 10.1021/acs.biochem.5b00048. Epub 2015 Jun 2.

PMID:
25996254
5.

Cooperative binding of L-trp to human tryptophan 2,3-dioxygenase: resonance Raman spectroscopic analysis.

Fukumura E, Sugimoto H, Misumi Y, Ogura T, Shiro Y.

J Biochem. 2009 Apr;145(4):505-15. doi: 10.1093/jb/mvp002. Epub 2009 Jan 17.

PMID:
19218188
6.

Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase.

Capece L, Lewis-Ballester A, Marti MA, Estrin DA, Yeh SR.

Biochemistry. 2011 Dec 20;50(50):10910-8. doi: 10.1021/bi201439m. Epub 2011 Nov 23.

7.

How is the distal pocket of a heme protein optimized for binding of tryptophan?

Chauhan N, Basran J, Rafice SA, Efimov I, Millett ES, Mowat CG, Moody PC, Handa S, Raven EL.

FEBS J. 2012 Dec;279(24):4501-9. doi: 10.1111/febs.12036. Epub 2012 Nov 22.

8.

Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.

Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE.

Biochemistry. 2007 Jan 9;46(1):145-55.

PMID:
17198384
9.

The first step of the dioxygenation reaction carried out by tryptophan dioxygenase and indoleamine 2,3-dioxygenase as revealed by quantum mechanical/molecular mechanical studies.

Capece L, Lewis-Ballester A, Batabyal D, Di Russo N, Yeh SR, Estrin DA, Marti MA.

J Biol Inorg Chem. 2010 Aug;15(6):811-23. doi: 10.1007/s00775-010-0646-x. Epub 2010 Apr 2.

10.

Structural and functional analyses of human tryptophan 2,3-dioxygenase.

Meng B, Wu D, Gu J, Ouyang S, Ding W, Liu ZJ.

Proteins. 2014 Nov;82(11):3210-6. doi: 10.1002/prot.24653. Epub 2014 Aug 30.

PMID:
25066423
11.

ONIOM study on a missing piece in our understanding of heme chemistry: bacterial tryptophan 2,3-dioxygenase with dual oxidants.

Chung LW, Li X, Sugimoto H, Shiro Y, Morokuma K.

J Am Chem Soc. 2010 Sep 1;132(34):11993-2005. doi: 10.1021/ja103530v.

PMID:
20698527
12.

Structure and reaction mechanism in the heme dioxygenases.

Efimov I, Basran J, Thackray SJ, Handa S, Mowat CG, Raven EL.

Biochemistry. 2011 Apr 12;50(14):2717-24. doi: 10.1021/bi101732n. Epub 2011 Mar 18. Review.

13.

Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase.

Batabyal D, Yeh SR.

J Am Chem Soc. 2007 Dec 19;129(50):15690-701. Epub 2007 Nov 21.

PMID:
18027945
14.
15.
16.

Substrate stereo-specificity in tryptophan dioxygenase and indoleamine 2,3-dioxygenase.

Capece L, Arrar M, Roitberg AE, Yeh SR, Marti MA, Estrin DA.

Proteins. 2010 Nov 1;78(14):2961-72. doi: 10.1002/prot.22819.

17.

Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.

Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK.

Biochemistry. 2008 Oct 7;47(40):10677-84. doi: 10.1021/bi801202a. Epub 2008 Sep 11.

PMID:
18783250
18.

Expression and purification of recombinant human indoleamine 2, 3-dioxygenase.

Littlejohn TK, Takikawa O, Skylas D, Jamie JF, Walker MJ, Truscott RJ.

Protein Expr Purif. 2000 Jun;19(1):22-9.

PMID:
10833386
19.
20.

Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes.

Sono M, Taniguchi T, Watanabe Y, Hayaishi O.

J Biol Chem. 1980 Feb 25;255(4):1339-45. No abstract available.

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