Information on EC 4.1.1.83 - 4-hydroxyphenylacetate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.83
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxyphenylacetate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2
show the reaction diagram
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tyrosine degradation IV (to 4-methylphenol)
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4-hydroxyphenylacetate degradation
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SYSTEMATIC NAME
IUBMB Comments
4-(hydroxyphenyl)acetate carboxy-lyase (4-methylphenol-forming)
The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
340137-18-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 957
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3,4-dihydroxyphenyl)acetate + H+
4-methylcatechol + CO2
show the reaction diagram
(4-hydroxyphenyl)acetate + H+
4-methylphenol + CO2
show the reaction diagram
4-hydroxyphenylacetate + H+
4-cresol + CO2
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylacetate + H+
4-cresol + CO2
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
the gamma-subunit contains two [4Fe-4S] clusters
[4Fe-4S]-center
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the enzyme binds a maximum of two [4Fe-4S]2+/+ clusters
additional information
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indications for an as yet unidentified low molecular weight cofactor that is required for catalytic activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3,4-dihydroxyphenyl)acetate
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4-hydroxymandelate
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4-Hydroxyphenylacetamide
NaCl
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800 mM, 50% inactivation
O2
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readily and irreversibly inhibited
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
(3,4-dihydroxyphenyl)acetate
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-
0.358 - 2.8
(4-hydroxyphenyl)acetate
0.388 - 0.41
3,4-Dihydroxyphenylacetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110 - 135
(4-hydroxyphenyl)acetate
65 - 67
3,4-Dihydroxyphenylacetate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
(3,4-dihydroxyphenyl)acetate
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0.48
4-hydroxymandelate
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0.7
4-Hydroxyphenylacetamide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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x * 36000, SDS-PAGE
99500
2 * 100000 + 2 * 99500
100000
2 * 100000 + 2 * 99500
105000
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alpha,alpha‘, the smaller unit is a C-terminally truncated form, 1 * 110000 + 1 * 105000, SDS-PAGE
110000
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alpha,alpha‘, the smaller unit is a C-terminally truncated form, 1 * 110000 + 1 * 105000, SDS-PAGE
200000
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gel filtration
440000
445000
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SDS-PAGE
460000
hetero-octameric catalytically competent complex, gel filtration; hetero-octameric catalytically competent complex, gel filtration; hetero-octameric catalytically competent complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 36000, SDS-PAGE
heterooctamer
heterotetramer
2 * 100000 + 2 * 99500
octamer
beta4gamma4, small subunit HpdC has a molecular weight of 9598 Da as determined by MALDI TOF MS, the recombinant enzyme is a hetero-octameric catalytically competent complex; beta4gamma4, small subunit HpdC has a molecular weight of 9598 Da as determined by MALDI TOF MS, the recombinant enzyme is a hetero-octameric catalytically competent complex; beta4gamma4, small subunit HpdC has a molecular weight of 9598 Da as determined by MALDI TOF MS, the recombinant enzyme is a hetero-octameric catalytically competent complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation of the small subunit is responsible for th change in oligomeric state from inactive homo-dimeric protein of Clostridium difficile to the recombinant hetero-octameric catalytically competent complex; phosphorylation of the small subunit is responsible for th change in oligomeric state from inactive homo-dimeric protein of Clostridium difficile to the recombinant hetero-octameric catalytically competent complex; phosphorylation of the small subunit is responsible for th change in oligomeric state from inactive homo-dimeric protein of Clostridium difficile to the recombinant hetero-octameric catalytically competent complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 22% (w/v) PEG MME 550, 30 mM MgCl2, 100 mM Tris/HCl pH 7.5-8.4
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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0°C in presence of 1 mM sodium sulfide and 5 mM ammonium sulfate
658599
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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half-life: 15 min, in presence of 1 mM sodium sulfide and 5 mM ammonium sulfate
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
readily and irreversibly inhibited by O2
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658599
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 100 mM Tris/HCl, pH 7.5, 5 mM ammonium sulfate, 1 mM magnesium chloride, more than 90% of the activity is recovered after 5 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Streptactin-Macroprep column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of three genes encoding two subunits of the glycyl-radical enzyme and the activating enzyme, expressed in Escherichia coli; cloning of three genes encoding two subunits of the glycyl-radical enzyme and the activating enzyme, expressed in Escherichia coli; cloning of three genes encoding two subunits of the glycyl-radical enzyme and the activating enzyme, expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli Rosetta (DE3) pLysS cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Show AA Sequence (489 entries)
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