Literature summary for 2.3.1.16 extracted from

Pye, V.E.; Christensen, C.E.; Dyer, J.H.; Arent, S.; Henriksen, A.
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch (2010), J. Biol. Chem., 285, 24078-24088.

Search for more literature for 2.3.1.16

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state	Arabidopsis thaliana
to 1.8 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state	Helianthus annuus

Inhibitors

Inhibitors	Comment	Organism	Structure
cystamine	10 mM, inactivation with half-life of 0.6 h	Arabidopsis thaliana
additional information	in presence of 20 mM cysteamine, full activity is maintained for more than 12 h	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
peroxisome	-	Arabidopsis thaliana	5777	-
peroxisome	-	Helianthus annuus	5777	-

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q56WD9	-	-
Helianthus annuus	Q6W6X6	-	-

Storage Stability

Storage Stability	Organism
in the absence of both cystamine and cysteamine isoform KAT2 spontaneously inactivates with a half-life	Arabidopsis thaliana
of 2.6 h	Arabidopsis thaliana

Subunits

Subunits	Comment	Organism
More	enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling	Arabidopsis thaliana
More	enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling	Helianthus annuus

Synonyms

Synonyms	Comment	Organism
KAT2	-	Arabidopsis thaliana
KAT2	-	Helianthus annuus

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Release 2023.1 (January 2023)