PMID:19015259

Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator).

Direct TIGAR biochemistry establishes donor activity and substrate discrimination, not the substrate of the Arabidopsis protein.

"The recombinant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro."

Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features.

file:ARATH/AT4G38370/AT4G38370-bioinformatics/RESULTS.md

Exploratory exact-input alignment to the experimentally characterized TIGAR donor

file:ARATH/AT4G38370/AT4G38370-bioinformatics/RESULTS-rereview.md

Re-review entry identity and catalytic-residue mapping for AT4G38370

file:ARATH/AT4G38370/AT4G38370-deep-research-falcon.md

Falcon deep research report for AT4G38370

file:ARATH/AT4G38370/AT4G38370-prediction-donor.json

UniProt identification of the structure-matched TIGAR donor

file:ARATH/AT4G38370/AT4G38370-protnlm-source.json

Frozen exact-input ProtNLM output and UniProt sequence for Q0WW53