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Information on EC 4.1.1.4 - acetoacetate decarboxylase and Organism(s) Chromobacterium violaceum and UniProt Accession Q7NSA6

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.4 acetoacetate decarboxylase
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Select one or more organisms in this record: ?
This record set is specific for:
Chromobacterium violaceum
UNIPROT: Q7NSA6 not found.
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Word Map
The taxonomic range for the selected organisms is: Chromobacterium violaceum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
acetoacetate decarboxylase, aadase, acetoacetic acid decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AAD
-
-
-
-
Acetoacetic decarboxylase
-
-
-
-
ADC
-
-
-
-
CP 28/CP 29
-
-
-
-
Decarboxylase, acetoacetate
-
-
-
-
Polymyxin MI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acetoacetate carboxy-lyase (acetone-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-03-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-pentanedione
?
show the reaction diagram
-
-
-
?
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Pentanedione
potent inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.7
acetoacetate
at 25°C, in 50 mM phosphate buffer, pH 5.95
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
349
acetoacetate
at 25°C, in 50 mM phosphate buffer, pH 5.95
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodecamer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AAD complexed with 2,4-pentanedione, hanging drop vapor diffusion method, using 18-20% (v/v) glycerol, 40 mM phosphate buffer, pH 5.95, 100 mM sarcosine and 14-15% (w/v) PEG 3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E61Q
the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)
R29Q
the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ho, M.C.; Menetret, J.F.; Tsuruta, H.; Allen, K.N.
The origin of the electrostatic perturbation in acetoacetate decarboxylase
Nature
459
393-397
2009
Clostridium acetobutylicum (P23670), Chromobacterium violaceum (Q7NSA6)
Manually annotated by BRENDA team
Ishikita, H.
Origin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase
FEBS Lett.
584
3464-3468
2010
Clostridium acetobutylicum (P23670), Chromobacterium violaceum (Q7NSA6)
Manually annotated by BRENDA team