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

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(→‎15-LOX Parameters)
(→‎15-LOX Parameters)
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{|class="wikitable sortable"  
 
{|class="wikitable sortable"  
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|+  style="text-align: left;" | Enzyme Concentrations
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|+  style="text-align: left;" | 15-LOX Abundance
 
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! Value
 
! Value
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! Reference
 
! Reference
 
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|-
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|1.60e-05 - 4.00e-05
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|4.09
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|mM
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|<math> ppm </math>
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|Human
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|Human  
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|Human reticulocyte 15-lipoxygenase-1, Enzymatic assays were performed in 25 mM Hepes buffer (pH 7.5,
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|Expression Vector: Lung
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25C), with and without product (12-HETE) addition, in the presence of 25 μM of substrate.
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Enzyme: 15-LOX
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|<ref name="Wecksler2009"> [www.ncbi.nlm.nih.gov/pubmed/19469483 Wecksler A. "Mechanistic Investigations of Human Reticulocyte 15- and Platelet 12-Lipoxygenases with Arachidonic Acid'' Biochemistry, 2009, 48 (26), pp 6259–6267]</ref>
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pH: 7.5
 +
Temperature: 37 °C
 +
|<ref name="Kim2014"> [http://www.nature.com/nature/journal/v509/n7502/pdf/nature13302.pdf M. Kim ''A draft map of the human proteome'' Nature, 2014 509, 575–581]</ref>
 +
|-
 +
|37.4
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|<math> ppm </math>
 +
|Human
 +
|Expression Vector: Spleen
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Enzyme: 15-LOX
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pH: 7.5
 +
Temperature: 37 °C
 +
|<ref name="Wilhelm2014"> [http://www.nature.com/nature/journal/v509/n7502/pdf/nature13319.pdf M. Wilhelm ''Mass-spectrometry-based draft of the human proteome'' Nature, 2014 509, 582–587]</ref>
 
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|-
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|2.00e-05
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|1.40
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|mM
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|<math> ppm </math>
 
|Human  
 
|Human  
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|Epithelium
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|Expression Vector: Gut
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|<ref name="Jacquot2008"> [http://www.ncbi.nlm.nih.gov/pubmed/18547056 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.]</ref> _
+
Enzyme: 12-LOX
 +
pH: 7.5
 +
Temperature: 37 °C
 +
|<ref name="Kim2014"> [http://www.nature.com/nature/journal/v509/n7502/pdf/nature13302.pdf M. Kim ''A draft map of the human proteome'' Nature, 2014 509, 575–581]</ref>
 +
|-
 
|}
 
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Revision as of 11:42, 12 August 2016

Return to overview

Reaction

R17 AA - HPETE15.jpg

Chemical equation

AA \rightleftharpoons PGH2

Rate equation

15-LOX Parameters

Michaelis-Menten Constants
Value Units Species Notes Reference
3.70E-03 ± 3.00E-04 mM Human Expression Vector: Epithelium

Enzyme: 15-Lipoxygenase pH: 7.5 Temperature: 25

[1]
5.00E-03 mM Human Expression Vector: Reticulocyte

Enzyme: 15-Lipoxygenase pH:7.5 Temperature: Unspecified

[2]
1.06E-02 mM Human Expression Vector: Keratinocyte

Enzyme: 15-Lipoxygenase pH: 6.7 - 7.3 Temperature: 37

[3]
1.17E-02 ± 9.00E-04 mM Human Expression Vector: Baculovirus Insect Cell

Enzyme: Wildtype 15-Lipoxygenase pH: 6.8 Temperature: 37

[4]
Enzyme Turnover Numbers
Value Units Species Notes Reference
595.8 ± 16.8 minute^{-1} Human Expression Vector: Epithelium

Enzyme: 15-Lipoxygenase pH: 7.5 Temperature: 25

[1]
37.2 ± 1.8 per minute Expression Vector:Human prostate epithelial

Enzyme:15-lipoxygenase-2

pH 7, Temperature: 22 [5]
45 ± 1.2 pH 7.5, Temperature: 22
44.4 ± 2.4 pH 8, Temperature: 22
34.2 ± 0.6 15°C, pH = 7.5
45 ± 1.2 22°C, pH = 7.5
62.4 ± 4.2 30°C, pH = 7.5
82.8 ± 4.8 37°C, pH = 7.5
15-LOX Abundance
Value Units Species Notes Reference
4.09 ppm Human Expression Vector: Lung

Enzyme: 15-LOX pH: 7.5 Temperature: 37 °C

[6]
37.4 ppm Human Expression Vector: Spleen

Enzyme: 15-LOX pH: 7.5 Temperature: 37 °C

[7]
1.40 ppm Human Expression Vector: Gut

Enzyme: 12-LOX pH: 7.5 Temperature: 37 °C

[6]

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. ↑ Wecksler A. "Kinetic and Structural Investigations of the Allosteric Site in Human Epithelial 15-Lipoxygenase-2 Biochemistry, 2009, 48 (36), pp 8721–8730
  6. ↑ 6.0 6.1 M. Kim A draft map of the human proteome Nature, 2014 509, 575–581
  7. ↑ M. Wilhelm Mass-spectrometry-based draft of the human proteome Nature, 2014 509, 582–587

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