Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterodimer
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
?
x * 72821, calculated
?
x * 70000, recombinant enzyme, SDS-PAGE
?
-
x * 24000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
?
-
x * 54000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
?
x * 78000, calculated from the deduced amino acid sequence
?
x * 74000, about, sequence calculation, ADC1
?
x * 70600, about, recombinant His6-tagged enzyme, sequence calculation
?
-
x * 70600, about, recombinant His6-tagged enzyme, sequence calculation
-
?
x * 74500, about, sequence calcualtion of His-tagged isozyme Adc1
?
x * 78200, about, sequence calcualtion of His-tagged isozyme Adc2
decamer
-
decamer dissociates in stages rather than all at once to a dimer
decamer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
decamer
-
10 * 82000-96000, SDS-PAGE
decamer
-
10 * or 1 * 82000, degradative arginine decarboxylase
decamer
pentamer of homodimers, X-ray crystallography
decamer
-
10 * 82000-96000, SDS-PAGE
-
decamer
(alphabeta)5, 10 * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE
decamer
-
(alphabeta)5, 10 * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE
-
dimer
the enzyme is a head-to-tail homodimer with two active sites acting in trans across the interface of the dimer
dimer
isozymes AtADC1 and AtADC2 are able to form homodimers in the cytosol and chloroplast. The formation of AtADC1/AtADC2 heterodimers occurs with similar subcellular localization than homodimers. Both ADC proteins are located in the same cell compartments, and they are able to form protein interaction complexes with each other
dimer
-
decamer dissociates in stages rather than all at once to a dimer
dimer
-
2 * or 10 * 82000, degradative arginine decarboxylase
dimer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
dimer
stabilized by two inter-subunit disulfide bonds, structural modeling
dimer
the enzyme dimer is stablized by the disulfide bridge involving Cys196
dimer
-
in solution at pH 8.0, light-scattering analysis
hexamer
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
hexamer
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
-
hexamer
6 * 68000, about, recombinant His-tagged enzyme, SDS-PAGE
hexamer
-
6 * 68000, about, recombinant His-tagged enzyme, SDS-PAGE
-
hexamer
-
6 * 36000-36500, SDS-PAGE
hexamer
-
3 * alpha 11000-13000 + 3 * beta 5000-7000, SDS-PAGE
hexamer
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
octamer
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
octamer
-
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
-
tetramer
x-ray crystallography
tetramer
-
x-ray crystallography
-
tetramer
-
4 * 78000, subunit mass calculated from the deduced amino acid sequence, SDS-PAGE
tetramer
-
4 * 74000, biosynthetic arginine decarboxylase
tetramer
x-ray crystallography
tetramer
-
4 * 58900, SDS-PAGE
tetramer
-
4 * 58900, SDS-PAGE
-
tetramer
x-ray crystallography
tetramer
-
4 * 74000, crystal structure analysis
trimer
-
3 * 74000, SDS-PAGE
trimer
Mutant E109Q, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. All 6 protomers are fully processed and contain the product agmatine at the active site. The presence of the product agmatine confirms that the mutant is active because the substrate arginine is added to the protein during crystallization.
trimer
Mutant N47A, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. The mutant protein does not show complete processing in all protomers. The first protomer of N47A is processed showing clear cleavage of the protomer to form the beta-chain (residues 1-52) and the alpha-chain (residues 53-165). A second protomer is unprocessed, showing clear density connecting residues Ser52 and Ser53. The final protomer in the first trimer can not easily be classified as either processed or unprocessed and is likely to be a mixture of the two states. The density between Ser52 and Ser53 is weak, density is also present corresponding to the pyruvoyl group and the product agmatine.
trimer
-
3 * 63000, SDS-PAGE
additional information
-
the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds
additional information
-
structural modelling
additional information
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
additional information
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
-
additional information
-
structural modelling
additional information
-
structural modelling
additional information
-
effects of substrate, coenzyme, and positive and negative effectors on the enzyme structure
additional information
Paramecium bursaria chlorella virus
-
the mobile loop, the K148-loop, is observed in a closed, substrate-bound conformation, this loop adopts different conformations throughout the catalytic cycle, overview
additional information
-
structural modelling
additional information
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
additional information
-
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
additional information
-
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
-
additional information
-
Synechocystis ADCs have a putative extra domain, which might be involved in the posttranslational regulation of ADC activity, structural modeling, overview
additional information
Synechocystis ADCs have a putative extra domain, which might be involved in the posttranslational regulation of ADC activity, structural modeling, overview
additional information
-
structural modelling
additional information
-
structural modelling
additional information
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview
additional information
-
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview