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Literature summary for 2.3.1.16 extracted from

  • Sundaramoorthy, R.; Micossi, E.; Alphey, M.S.; Germain, V.; Bryce, J.H.; Smith, S.M.; Leonard, G.A.; Hunter, W.N.
    The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation (2006), J. Mol. Biol., 359, 347-357.
    View publication on PubMed
Search for more literature for 2.3.1.16

Cloned(Commentary)

Cloned (Comment) Organism
expression of a His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues in Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution is mixed with 0.002 ml reservoir solution containing 0.1 M Tris–HCl, pH 8.5, 300 mM MgCl2, and 25% w/v polyethylene glycol 4000, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution Arabidopsis thaliana

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
 2 * 47000, recombinant detagged enzyme, SDS-PAGE Arabidopsis thaliana
100000
-
 recombinant detagged enzyme, gel filtration Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q56WD9 precursor
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification processing of the peroxisomal precursor protein Arabidopsis thaliana

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, His-tag removal by thrombin, to homogeneity Arabidopsis thaliana

Reaction

Reaction Comment Organism Reaction ID
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA the active site involves residues Cys138, in loop beta4–alpha3 on domain I, His393 on the segment linking alpha10 and alpha11 of domain III, and Cys425 at the C-terminal end of beta12, detailed reaction mechanism, overview Arabidopsis thaliana
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview Arabidopsis thaliana ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 47000, recombinant detagged enzyme, SDS-PAGE Arabidopsis thaliana
More crystal structure analysis, secondary structure, the enzyme shows a combination of two similar alpha/beta domains capped with a loop domain, comparison to the structure of the enzyme from Saccharomyces cerevisiae, overview Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
3-ketoacyl-CoA thiolase
-
 Arabidopsis thaliana
KAT
-
 Arabidopsis thaliana