4.1.1.11: aspartate 1-decarboxylase
This is an abbreviated version!
For detailed information about aspartate 1-decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.11
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4.1.1.11
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pantothenate
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pyrazinamide
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pyrazinoic
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self-processing
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pza-resistant
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synthesis
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drug development
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pharmacology
- 4.1.1.11
- pantothenate
- pyrazinamide
-
pyrazinoic
-
self-processing
-
pza-resistant
- synthesis
- drug development
- pharmacology
Reaction
Synonyms
ACD, ADC, ADCBs, ADCC.g, ADCCg, ADCE, Aspartate alpha-decarboxylase, aspartate decarboxylase, aspartate-alpha-decarboxylase, Aspartic alpha-decarboxylase, AspDC, BmADC, BsADC, CgADC, Dgad2, GcADC, L-Aspartate alpha-decarboxylase, L-Aspartate-alpha-decarboxylase, MfnA, MJ0050, More, MtbADC, PanD, PF1159, PLP-dependent L-aspartate decarboxylase, pyruvoyl-dependent l-aspartate alpha-decarboxylase, TK1814
ECTree
4.1.1.11 aspartate 1-decarboxylaseAdvanced search results
results (
results (Subunits
Subunits on EC 4.1.1.11 - aspartate 1-decarboxylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homotetramer
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
octamer
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two tetramers forming a pseudo fourfold rotational symmetry, the enzyme protein shows a double-psi beta-barrel structure
tetramer
additional information
?
x * 14100, pi-protein, calculated from the amino acid sequence
tetramer
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
tetramer
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the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
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tetramer
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
tetramer
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
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tetramer
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crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits
tetramer
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x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
tetramer
active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein
tetramer
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
tetramer
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active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein
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tetramer
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
tetramer
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
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tetramer
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4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE
tetramer
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4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE
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additional information
proform enzyme structure homology modeling, overview
additional information
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proform enzyme structure homology modeling, overview
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additional information
the Escherichia coli aspartate decarboxylase, ADC, is hexameric
additional information
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the Escherichia coli aspartate decarboxylase, ADC, is hexameric
additional information
Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1
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the Escherichia coli aspartate decarboxylase, ADC, is hexameric
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