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3b7s
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
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| + | Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design., Tholander F, Muroya A, Roques BP, Fournie-Zaluski MC, Thunnissen MM, Haeggstrom JZ, Chem Biol. 2008 Sep 22;15(9):920-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18804029 18804029] | ||
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Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17357161 17357161] | Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17357161 17357161] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 8 09:06:59 2008'' |
Revision as of 07:06, 8 October 2008
[E296Q]LTA4H in complex with RSR substrate
Template:ABSTRACT PUBMED 18804029
About this Structure
3B7S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design., Tholander F, Muroya A, Roques BP, Fournie-Zaluski MC, Thunnissen MM, Haeggstrom JZ, Chem Biol. 2008 Sep 22;15(9):920-9. PMID:18804029
Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:17357161
Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates., Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:15078870
Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:11675384
Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:11917124
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901
Page seeded by OCA on Wed Oct 8 09:06:59 2008
Categories: Homo sapiens | Single protein | Fournie-Zaluski, M C. | Haeggstrom, J. | Muroya, A. | Roques, B P. | Tholander, F. | Thunnissen, M. | Alternative splicing | Analogue peptide | Cytoplasm | Hydrolase | Hydrolysis | Leukotriene biosynthesis | Metal-binding | Metalloprotease | Multifunctional enzyme | Protease | Transition state | Tripeptide substrate | Zinc
