Difference between revisions of "Transformation of AA to 15-HPETE"

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|rowspan="3"|Human
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|rowspan="7"|Human prostate epithelial 15-lipoxygenase-2
 
|pH 7
 
|pH 7
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|rowspan="3"|<ref name="Wecksler2009"> [http://www.ncbi.nlm.nih.gov/pubmed/18547056 Jacquot C. "Kinetic and Structural Investigations of the Allosteric Site in Human Epithelial 15-Lipoxygenase-2'' Biochemistry, 2009, 48 (36), pp 8721–8730]</ref>  
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|rowspan="7"|<ref name="Wecksler2009"> [http://www.ncbi.nlm.nih.gov/pubmed/18547056 Jacquot C. "Kinetic and Structural Investigations of the Allosteric Site in Human Epithelial 15-Lipoxygenase-2'' Biochemistry, 2009, 48 (36), pp 8721–8730]</ref>  
 
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|45 ± 1.2
 
|45 ± 1.2
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|44.4 ± 2.4
 
|44.4 ± 2.4
 
|pH 8
 
|pH 8
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|34.2 ± 0.6
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|15
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|45 ± 1.2
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|22
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|62.4 ± 4.2
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|30
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|82.8 ± 4.8
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|37
 
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Revision as of 18:11, 10 April 2016

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Reaction

R17 AA - HPETE15.jpg

Chemical equation

AA \rightleftharpoons PGH2

Rate equation

Parameters

Michaelis-Menten Constants
Value Units Species Notes Reference
3.70E-03 ± 3.00E-04 mM Human Epithelium [1]
5.00E-03 mM Human Reticulocyte [2]
1.06E-02 mM Human Keratinocyte [3]
1.17E-02 ± 9.00E-04 mM Human Wildtype 15-Lipoxygenase [4]
Enzyme Turnover Numbers
Value Units Species Notes Reference
595.8 ± 16.8 minute^{-1} Human Epithelium [1]
37.2 ± 1.8 per minute Human prostate epithelial 15-lipoxygenase-2 pH 7 [5]
45 ± 1.2 pH 7.5
44.4 ± 2.4 pH 8
34.2 ± 0.6 15
45 ± 1.2 22
62.4 ± 4.2 30
82.8 ± 4.8 37

References

  1. ↑ 1.0 1.1 Jacquot C. "Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry. 2008 Jul 8;47(27):7295-303. doi: 10.1021/bi800308q. Epub 2008 Jun 12.
  2. ↑ Jacquot C. "Synthesis of 11-Thialinoleic Acid and 14-Thialinoleic Acid, Inhibitors of Soybean and Human Lipoxygenases Org Biomol Chem. 2008 Nov 21; 6(22): 4242–4252.
  3. ↑ Burrall B. "Enzymatic properties of the 15-lipoxygenase of human cultured keratinocytes. J Invest Dermatol. 1988 Oct;91(4):294-7.
  4. ↑ Sloane D. L. "Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: the side-chain geometry of amino acids 417 and 418 determine positional specificity. Protein Eng. 1995 Mar;8(3):275-82..
  5. ↑ Jacquot C. "Kinetic and Structural Investigations of the Allosteric Site in Human Epithelial 15-Lipoxygenase-2 Biochemistry, 2009, 48 (36), pp 8721–8730

Related Reactions

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