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Literature summary for 4.1.3.4 extracted from

  • Tuinstra, R.L.; Burgner, J.W.2nd.; Miziorko, H.M.
    Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase (2002), Arch. Biochem. Biophys., 408, 286-294.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 8fold stimulation at 5 mM Homo sapiens

Protein Variants

Protein Variants Comment Organism
C323S shows less dithiothreitol activation than wild-type enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Homo sapiens 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens last step in ketogenesis ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
107
-
C323S mutant Homo sapiens
114
-
wild-type Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-Hydroxy-3-methylglutaryl-CoA
-
Homo sapiens Acetyl-CoA + acetoacetate
-
?
additional information last step in ketogenesis Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer crosslinking experiments with dibromopopanone Homo sapiens
tetramer analytical ultracentrifugation, enzyme exists as a mixture of dimers and tetramers Homo sapiens