Difference between revisions of "Transformation of 15-Keto-PGE2 to 13,14-Dihydro-15-Keto-PGE2"

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! Reference
 
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| 3.6006165
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| kcal/mol
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|Unspecified
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|Calculations with a Gaussian98 suite of programs
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Enzyme: COX (Unspecific)
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Substrate: Arachidonate
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Temperature: 298.15 K
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Pressure: 1 bar
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|<ref name="Silva2003”>[http://link.springer.com/article/10.1007/s00214-003-0476-9 P. Silva, "A theoretical study of radical-only and combined radical/carbocationic mechanisms of arachidonic acid cyclooxygenation by prostaglandin H synthase" Theor Chem Acc (2003) 110: 345]</ref>
 
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Revision as of 16:00, 15 March 2017

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Reaction

Chemical equation

 15-Keto-PGE2 + NAD(P)+ \rightleftharpoons 13,14-Dihydro-15-Keto-PGE2 + NAD(P)H

Rate equation

Parameters

Michaelis-Menten Constants
Value Units Species Notes Reference
0.01121 ± 0.00014 mM Human Method: In vitro

Organism: Human Expression vector: E.coli Enzyme: PTGR2 pH: 7.5 Temperature: 37 ◦C Substrate: 15-Keto-PGE2

"For determining the KM and Vmax values for NADPH, 15-keto-PGE2 at a final concentration of 200 mM was used with different concentrations of NADPH (0–60 mM)."

[1]
0.01587 ± 0.00171 mM Human Method: In vitro

Organism: Human Expression vector: E.coli Enzyme: e PTGR2 pH: 7.5 Temperature: 37 ◦C Substrate: NADPH

"For determining the KM and Vmax values for NADPH, 15-keto-PGE2 at a final concentration of 200 mM was used with different concentrations of NADPH (0–60 mM)."

[1]
0.0496 ± 0.0058 mM Mouse Method: In vitro

Organism: Mouse Expression vector: Enzyme: 13,14-dehydro-15-oxoprostaglandin 13-reductase pH: 7.4 Temperature: 37 ◦C Substrate: 15-Ketoprostaglandin E2

[1]

Note: Turnover values from EC 1.3.1.48 - 13,14-dehydro-15-oxoprostaglandin 13-reductase

Enzyme Turnover Number
Value Units Species Notes Reference
11.4 ± 0.9 min-1 Mouse Method: In vitro

Organism: Mouse Expression vector: Enzyme: 13,14-dehydro-15-oxoprostaglandin 13-reductase pH: 7.4 Temperature: 37 ◦C Substrate: 15-Ketoprostaglandin E2

[1]


5-HEDH Abundance
Value Units Species Notes Reference
162 ppm Human Expression Vector: Skin

Enzyme: PTGR2 pH: 7.5 Temperature: 37 °C

[2]
80.9 ppm Human Expression Vector: Skin

Enzyme: PTGR2 pH: Unknown Temperature: Unknown

Unknown
74.1 ppm Human Expression Vector: Oral Cavity

Enzyme: PTGR2 pH: 7.5 Temperature: 37 °C

[2]
Gibbs Free energy
Value Units Species Notes Reference
3.6006165 kcal/mol Unspecified Calculations with a Gaussian98 suite of programs

Enzyme: COX (Unspecific) Substrate: Arachidonate Temperature: 298.15 K Pressure: 1 bar

[3]


Half Life
Value Units Species Notes Reference
9.9 +/-0.2 minutes Dog In vivo

Temperature:37 pH:7

[4]
Vmax
Value Units Species Notes Reference
159.23 ± 0.71 nmol min-1 mg-1 Human Method: In vitro

Organism: Human Expression vector: E.coli Enzyme: PTGR2 pH: 7.5 Temperature: 37 ◦C Substrate: 15-Keto-PGE2

[1]
66.73 ± 1.36 nmol min-1 mg-1 Human Method: In vitro

Organism: Human Expression vector: E.coli Enzyme: PTGR2 pH: 7.5 Temperature: 37 ◦C Substrate: NADPH

[1]

References

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2, Structure. 2008 Nov 12;16(11):1714-23. doi: 10.1016/j.str.2008.09.007. Cite error: Invalid <ref> tag; name "Wu2008" defined multiple times with different content Cite error: Invalid <ref> tag; name "Wu2008" defined multiple times with different content Cite error: Invalid <ref> tag; name "Wu2008" defined multiple times with different content Cite error: Invalid <ref> tag; name "Wu2008" defined multiple times with different content
  2. 2.0 2.1 [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]
  3. P. Silva, "A theoretical study of radical-only and combined radical/carbocationic mechanisms of arachidonic acid cyclooxygenation by prostaglandin H synthase" Theor Chem Acc (2003) 110: 345
  4. W. Bothwell, "A radioimmunoassay for the unstable pulmonary metabolites of prostaglandin E1 and E2: an indirect index of their in vivo disposition and pharmacokinetics" Journal of Pharmacology and Experimental Therapeutics February 1982, 220 (2) 229-235