Claim · model-written summary
Glucose noncompetitively inhibited invertase.
- Taxon
- Pteris deflexa
Pteris deflexat0 - Treatment
- glucosee0
- Outcome
- non-competitive inhibitorse0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively.”
t0“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
Title
Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity
J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450
Other claims from this paper (11)
- Intervention effect Fructose competitively inhibited invertase.
- Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
- Observation The purified invertase was a heterodimer with two reported subunit sizes.
- Observation The invertase had beta-fructofuranosidase activity.
- Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
- Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
- Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
- Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
- Observation Pinnas had the highest invertase levels.
- Observation Invertase was localized mainly in phloem cells.
- Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.