Difference between revisions of "Transformation of AA to PGH2"

From ISMOC
Jump to: navigation, search
(→‎COX-2 Enzyme Parameters)
(→‎COX-2 Enzyme Parameters)
Line 9: Line 9:
  
 
== Rate equation ==
 
== Rate equation ==
 +
 +
 +
== COX-1 Enzyme Parameters ==
 +
{|class="wikitable sortable"
 +
|+  style="text-align: left;" | COX-2 Michaelis-Menten Constants (When AA is the substrate)
 +
|-
 +
! Value
 +
! Units
 +
! Species
 +
! Notes
 +
! Reference
 +
|-
 +
|0.0088 ± 0.0022
 +
|<math> mM </math>
 +
|Human
 +
|Expression Vector: Human
 +
Enzyme: Cyclooxygenase-1
 +
pH: 7.6 - 8.4
 +
Temperature: 37 °C
 +
|<ref name="Noreen1998"> [http://pubs.acs.org/doi/abs/10.1021/np970343j Y. ''Noreen Development of a Radiochemical Cyclooxygenase-1 and -2 in Vitro Assay for Identification of Natural Products as Inhibitors of Prostaglandin Biosynthesis''J. Nat. Prod., 1998, 61 (1), pp 2–7)]</ref>
 +
|-
 +
 +
|}
 +
  
  
Line 14: Line 38:
  
 
{|class="wikitable sortable"  
 
{|class="wikitable sortable"  
−
|+  style="text-align: left;" | Michaelis-Menten Constants (When AA is the substrate)
+
|+  style="text-align: left;" | COX-2 Michaelis-Menten Constants (When AA is the substrate)
 
|-
 
|-
 
! Value
 
! Value

Revision as of 15:18, 21 July 2016

Return to overview

Reaction

R2 AA-PGH2.jpg

Chemical equation

AA \rightleftharpoons PGH2

Rate equation

COX-1 Enzyme Parameters

COX-2 Michaelis-Menten Constants (When AA is the substrate)
Value Units Species Notes Reference
0.0088 ± 0.0022 mM Human Expression Vector: Human

Enzyme: Cyclooxygenase-1 pH: 7.6 - 8.4 Temperature: 37 °C

[1]


COX-2 Enzyme Parameters

COX-2 Michaelis-Menten Constants (When AA is the substrate)
Value Units Species Notes Reference
1.62E-02 ± 0.22E-02 mM Human Expression Vector: Embryonic kidney cells

Enzyme: Cyclooxygenase-2 pH: Not specified Temperature: Not specified

[2]
5.14E-03 ± 2.90E-04 mM Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
2.1E-03 ± 4.00E-04 mM Human Expression Vector: E. Coli

Enzyme: Wild Type Cyclooxygenase-2 Enzyme pH: 8.5 Temperature:30 °C

[4]
2.1E-03 ± 4.00E-04 mM Human Expression Vector: Baculuvirus

Enzyme: Wild Type Cycloxygenase-2 pH: 7.2 Temperature: 30 °C 100 uM arachidonate substrate,

[5]
Enzyme Turnover Numbers (When AA is the substrate)
Value Units Species Notes Reference
1620 ± 24 per minute Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
Michaelis-Menten Constants (When EPA is the substrate)
Value Units Species Notes Reference
9.45E-03 ± 7.30E-04 mM Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
Enzyme Turnover Numbers (When EPA is the substrate)
Value Units Species Notes Reference
522 ± 12.6 per minute Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
Michaelis-Menten Constants (When DHA is the substrate)
Value Units Species Notes Reference
3.68E-02 ± 4.25E-03 mM Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
Enzyme Turnover Numbers (When DHA is the substrate)
Value Units Species Notes Reference
207 ± 9 per minute Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]
Enzyme Concentration
Value Units Species Notes Reference
1.45e-02 mM Mouse Expression Vector: Baculovirus (Insect Cell)

Enzyme: COX-2 pH: 8.0 Temperature: 37 °C 1–200 µM of substrate.

[3]

References

  1. ↑ Y. Noreen Development of a Radiochemical Cyclooxygenase-1 and -2 in Vitro Assay for Identification of Natural Products as Inhibitors of Prostaglandin BiosynthesisJ. Nat. Prod., 1998, 61 (1), pp 2–7)
  2. ↑ S.F. Kim Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 2005,310(5756):1966-70)
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 [www.ncbi.nlm.nih.gov/pubmed/20463020 Vecchio A. J. "Structural basis of fatty acid substrate binding to cyclooxygenase-2." J. Biol. Chem. 285 22152-63 (2010)]
  4. ↑ [http://pubs.acs.org/doi/pdf/10.1021/bi035717o Rogge C. "Identification of Tyr504 as an Alternative Tyrosyl Radical Site in Human Prostaglandin H Synthase-2" Biochemistry 2004, 43, 1560-1568]
  5. ↑ [http://www.jbc.org/content/279/6/4084.full.pdf Bambai B. "Role of Asn-382 and Thr-383 in Activation and Inactivation of Human Prostaglandin H Synthase Cyclooxygenase Catalysis" February 6, 2004 The Journal of Biological Chemistry, 279, 4084-4092.]

Related Reactions

Retrieved from ‘http://www.systemsbiology.ls.manchester.ac.uk/wiki/index.php?title=Transformation_of_AA_to_PGH2&oldid=4644’