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Literature summary for 3.2.1.26 extracted from

  • Hothorn, M.; Van den Ende, W.; Lammens, W.; Rybin, V.; Scheffzek, K.
    Structural insights into the pH-controlled targeting of plant cell-wall invertase by a specific inhibitor protein (2010), Proc. Natl. Acad. Sci. USA, 107, 17427-17432.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
2.6 A crystal structure of cell-wall invertase 1 in complex with a protein inhibitor, cell-wall inhibitor of beta-fructosidase, from tobacco. The structure recognizes a small amino acid motif in the inhibitor that directly targets the invertase active site. The activity of INV1 and its interaction with inhibitor are strictly pH-dependent with a maximum at about pH 4.5. At this pH, isothermal titration calorimetry reveals that the inhibitor tightly binds its target with nanomolar affinity. Cell wall inhibitor of beta-fructosidase competes with sucrose for the same binding site Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
cellwall inhibitor of beta-fructosidase 2.6 A crystal structure of cell-wall invertase 1 in complex with protein inhibitor, cell-wall inhibitor of beta-fructosidase, from tobacco. The structure recognizes a small amino acid motif in the inhibitor that directly targets the invertase active site. The activity of INV1 and its interaction with inhibitor are strictly pH-dependent with a maximum at about pH 4.5. At this pH, isothermal titration calorimetry reveals that the inhibitor tightly binds its target with nanomolar affinity Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q43866
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-

Synonyms

Synonyms Comment Organism
cwINV1
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Arabidopsis thaliana