1h19: Difference between revisions
New page: left|200px<br /> <applet load="1h19" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h19, resolution 2.1Å" /> '''STRUCTURE OF [E271Q]... |
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==About this Structure== | ==About this Structure== | ||
1H19 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN, YB, IMD and ACY as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H19 OCA]]. | 1H19 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN, YB, IMD and ACY as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6]]. Structure known Active Site: ZN1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H19 OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11675384 11675384] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11675384 11675384] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Leukotriene-A(4) hydrolase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Haeggstrom, J.Z.]] | [[Category: Haeggstrom, J.Z.]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:07:50 2007'' | ||
Revision as of 12:03, 30 October 2007
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STRUCTURE OF [E271Q] LEUKOTRIENE A4 HYDROLASE
OverviewOverview
Leukotriene A(4) hydrolase/aminopeptidase is a bifunctional zinc, metalloenzyme that converts the fatty acid epoxide leukotriene A(4) into, leukotriene B(4), a potent chemoattractant and immune-modulating lipid, mediator. Recently, the structure of leukotriene A(4) hydrolase revealed, that Glu-271, which belongs to a conserved GXMEN motif in the M1 family of, zinc peptidases, and Gln-136 are located at the active site. Here we, report that mutagenetic replacements of Glu-271, but not Gln-136, abrogate, both catalytic activities of leukotriene A(4) hydrolase. Furthermore, the, 2.1 A crystal structure of [E271Q]leukotriene A(4) hydrolase revealed, minimal conformational changes that could not explain the loss of enzyme, function. We propose that the carboxylate of Glu-271 participates in ... [(full description)]
About this StructureAbout this Structure
1H19 is a [Single protein] structure of sequence from [Homo sapiens] with ZN, YB, IMD and ACY as [ligands]. Active as [Leukotriene-A(4) hydrolase], with EC number [3.3.2.6]. Structure known Active Site: ZN1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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