The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation

Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
Proteins: Structure, Function, and Bioinformatics (2025 Jan 23)

doi: 10.1002/prot.26803

Submitted to SASBDB: 2024 Jul 30 Published in SASBDB: 2025 Jan 20

SASDVW5 – alpha-amylase AMY3 Sample: Alpha-amylase 3, chloroplastic dimer, 187 kDa Arabidopsis thaliana protein Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16 RgGuinier 5.1 nm Dmax 21.5 nm VolumePorod 444 nm3

SASDVX5 – pseudoamylase BAM9 Sample: Inactive beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16 RgGuinier 2.4 nm Dmax 8.7 nm VolumePorod 87 nm3

SASDVY5 – pseudoamylase BAM9 bound to alpha-amylase AMY3 Sample: Inactive beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein Alpha-amylase 3, chloroplastic monomer, 94 kDa Arabidopsis thaliana protein Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16 RgGuinier 5.0 nm Dmax 25.5 nm VolumePorod 380 nm3