Difference between revisions of "Transformation of 15-Keto-PGE2 to 13,14-Dihydro-15-Keto-PGE2"
(→Parameters) |
(→Parameters) |
||
Line 23: | Line 23: | ||
! Reference | ! Reference | ||
|- | |- | ||
− | | 0. | + | | 0.01121 ± 0.00014 |
| mM | | mM | ||
− | + | | Human | |
− | + | |Method: In vitro | |
− | |||
− | |||
− | |||
− | |||
− | | Human | ||
− | | | ||
− | Method: In vitro | ||
Organism: Human | Organism: Human | ||
− | Expression vector: | + | Expression vector: E.coli |
− | Enzyme: | + | Enzyme: PTGR2 |
− | pH: 7. | + | pH: 7.5 |
− | Temperature: 37 ◦C | + | Temperature: 37 ◦C |
− | | <ref name=" | + | 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)." | ||
+ | |||
+ | | <ref name="Wu2008"> [https://www.ncbi.nlm.nih.gov/pubmed/19000823 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.]</ref> | ||
|- | |- | ||
− | | 0. | + | |0.01587 ± 0.00171 |
− | | mM | + | |mM |
− | | Human | + | |Human |
− | | | + | |Method: In vitro |
− | Method: In vitro | ||
Organism: Human | Organism: Human | ||
− | Expression vector: | + | Expression vector: E.coli |
− | Enzyme: | + | Enzyme: e PTGR2 |
− | pH: 7. | + | pH: 7.5 |
− | Temperature: 37 ◦C | + | Temperature: 37 ◦C |
− | + | Substrate: NADPH | |
− | and | + | |
− | + | "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)." | ||
− | + | | <ref name="Wu2008"> [https://www.ncbi.nlm.nih.gov/pubmed/19000823 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.]</ref> | |
− | |||
− | |||
− | |||
− | |||
− | |||
− | |||
|- | |- | ||
− | + | ||
− | |||
− | |||
− | |||
− | |||
|} | |} | ||
+ | |||
+ | |||
{|class="wikitable" | {|class="wikitable" |
Revision as of 10:27, 13 March 2017
Reaction
Chemical equation
Rate equation
Parameters
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] |
Value | Units | Species | Notes | Reference |
---|---|---|---|---|
X | Y | Z | A | B |
Value | Units | Species | Notes | Reference |
---|---|---|---|---|
X | Y | Z | A | B |
Value | Units | Species | Notes | Reference |
---|---|---|---|---|
X | Y | Z | A | B |
Value | Units | Species | Notes | Reference |
---|---|---|---|---|
9.9 +/-0.2 | minutes | Dog | In vivo
Temperature:37 pH:7 |
[2] |
- ↑ 1.0 1.1 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.
- ↑ 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