Difference between revisions of "Transformation of AA to PGH2"

Revision as of 17:34, 11 April 2016

AA \rightleftharpoons PGH2

Michaelis-Menten Constants (When AA is the substrate)
Value	Units	Species	Notes	Reference
1.62E-02	$mM$	Human	X	^[1]
5.14E-03 ± 2.90E-04	mM	Mouse	In vitro,	^[2]
2.1E-03 ± 4.00E-04	mM	Human	Wild Type Enzyme Assay, 30 °C	^[3]
2.1E-03 ± 4.00E-04	mM	Human	Wild Type cycloxygenase activty, 100 �M arachidonate substrate, pH 7.2.	^[4]

Enzyme Turnover Numbers (When AA is the substrate)
Value	Units	Species	Notes	Reference
1620 ± 24	per minute	Mouse	In vitro, 37 °C, pH 8.0, 1–200 µM of substrate.	^[2]

Michaelis-Menten Constants (When EPA is the substrate)
Value	Units	Species	Notes	Reference
9.45E-03 ± 7.30E-04	mM	Mouse	In vitro,	^[2]

Enzyme Turnover Numbers (When EPA is the substrate)
Value	Units	Species	Notes	Reference
522 ± 12.6	per minute	Mouse	In vitro, 37 °C, pH 8.0, 1–200 µM of substrate.	^[2]

Michaelis-Menten Constants (When DHA is the substrate)
Value	Units	Species	Notes	Reference
3.68E-02 ± 4.25E-03	mM	Mouse	In vitro,	^[2]

Enzyme Turnover Numbers (When DHA is the substrate)
Value	Units	Species	Notes	Reference
207 ± 9	per minute	Mouse	In vitro, 37 °C, pH 8.0, 1–200 µM of substrate.	^[2]

↑ S.F. Kim Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 2005,310(5756):1966-70)
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 [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)]
↑ [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]
↑ [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.]

@@ Line 33: / Line 33: @@
 |In vitro,
 |<ref name="Vecchoi2010"> [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)]</ref>
+|-
+|2.1E-03 ± 4.00E-04
+|mM
+|Human
+|Wild Type Enzyme Assay, 30 °C
+|<ref name="Rogge2003"> [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]</ref>
+|-
+|2.1E-03 ± 4.00E-04
+|mM
+|Human
+|Wild Type cycloxygenase activty, 100 �M arachidonate substrate, pH 7.2.
+|<ref name="Bambai2004"> [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.]</ref>
 |-
 |}
@@ Line 51: / Line 65: @@
 |<ref name="Vecchoi2010"> [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)]</ref>
 |-
 |}