Claim · model-written summary
Vestitone reductase showed strict stereospecificity for (3R)-vestitone, with Km 45 microM.
- Taxon
- alfalfa
Medicago sativat0 - Gene
- Vestitone reductasee0
- Outcome
- Km valuee0
- Value
- 45 microMe0
- Qualifier
- strict substrate stereo specificity for (3R)-vestitonee0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“alfalfa (Medicago sativa L.)”
e0“Vestitone reductase has strict substrate stereo specificity for (3R)-vestitone with a Km value of 45 microM”
Title
L. Guo; R.A. Dixon; N.L. Paiva Journal of Biological Chemistry 1994. doi:10.1016/s0021-9258(17)31799-4
Other claims from this paper (11)
- Mechanism Apparent pterocarpan synthase activity comprises two independent enzyme activities.
- Mechanism Vestitone reductase catalyzes NADPH-dependent reduction of vestitone to DMI.
- Mechanism DMI dehydratase catalyzes water loss and ether-ring closure to form medicarpin.
- Observation Vestitone reductase was purified 1,840-fold to homogeneity.
- Observation Vestitone reductase had an estimated SDS-PAGE molecular mass of 38 kDa.
- Observation Native vestitone reductase mass was 34 kDa, indicating a monomer.
- Observation DMI dehydratase was partially purified 962-fold.
- Observation DMI dehydratase had a native molecular mass of 38 kDa.
- Observation DMI dehydratase had Km 5 microM for DMI.
- Observation Both enzymes had a temperature optimum of 30 degrees C.
- Observation Both enzymes had a pH optimum of 6.0.