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heptamer
7 * 57000, SDS-PAGE
?
x * 57000, SDs-PAGE, His-tagged protein
?
-
x * 58000, SDS-PAGE
-
?
-
x * 62000 + x * 40000, gel filtration in presence of guanidine
?
-
? * 58000, identical subunits
?
-
x * 56000, canonical isoforms of IMPDH1 and smaller retinal isoform, x * 65000, large retinal isoform, calculated
?
-
multiples with a basic unit of 160000
?
x * 52900, calculated from sequence
dimer
-
2 * 38000, amino acid analysis
dimer
-
2 * 68000, Yoshida sarcoma ascites tumor cells, SDS-PAGE
homotetramer
4 * 38459, sequence calculation
homotetramer
-
4 * 38459, sequence calculation
-
homotetramer
-
small angle X-ray scattering
octamer
-
IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric
octamer
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IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric
-
octamer
the quaternary structure of the second class IMPDHbt oscillates between tetramer and octamer. IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric, while in the presence of NAD, IMPDHbt is predominantly octameric
tetramer
-
4 * 40435, long enzyme truncation CBS-mutant BaIMPDHDELTAL, sequence calculation, 4 * 37920, short enzyme truncation CBS-mutant BaIMPDHDELTAL, sequence calculation
tetramer
-
4 * 56000 gel filtration
tetramer
-
in the presence of IMP, class II IMPDHs remain tetrameric
tetramer
-
in the presence of IMP, class II IMPDHs remain tetrameric
-
tetramer
-
4 * 40722, short enzyme truncation CBS-mutant CjIMPDHDELTAS, sequence calculation
tetramer
-
4 * 38123, long enzyme truncation CBS-mutant ClpIMPDHDELTAL, sequence calculation
tetramer
small angle X-ray scattering
tetramer
enzyme structure in solution
tetramer
-
enzyme structure in solution
-
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 56000 density gradient centrifugation
tetramer
-
the enzyme forms a homotetramer with four active sites and an open dehydrogenase conformation
tetramer
-
4 * 55000, SDS-PAGE
tetramer
4 * 54775, mass spectrometry, x * 55000, recombinnat enzyme, SDS-PAGE, 4 * 54700, about, sequence calculation
tetramer
-
4 * 54775, mass spectrometry, x * 55000, recombinnat enzyme, SDS-PAGE, 4 * 54700, about, sequence calculation
-
tetramer
-
4 * 60000, rat hepatoma 3924 A cells, SDS-PAGE
tetramer
-
the enzyme contains a cystathione beta-synthase-like subdomain which is involved in nucleic acid binding
tetramer
-
the enzyme forms a homotetramer with four active sites
tetramer
-
4 * 37929, long enzyme truncation CBS-mutant VcIMPDHDELTAL, sequence calculation
tetramer
-
4 * 50000, SDS-PAGE
tetramer or octamer
Q81W29
in the presence of NAD+, IMPDHba is predominantly octameric
tetramer or octamer
-
in the case of IMPDHkp, several peaks are detected, which correspond to tetrameric species and higher oligomeric forms, multiples of tetramers, under equilibrium
tetramer or octamer
-
in the case of IMPDHkp, several peaks are detected, which correspond to tetrameric species and higher oligomeric forms, multiples of tetramers, under equilibrium
-
tetramer or octamer
the quaternary structure of the second class IMPDHsa oscillates between tetramer and octamer. Enzyme IMPDHsa is tetrameric in the apo state. In the presence of IMP, class II IMPDHs remain tetrameric
tetramer or octamer
-
the quaternary structure of the second class IMPDHsa oscillates between tetramer and octamer. Enzyme IMPDHsa is tetrameric in the apo state. In the presence of IMP, class II IMPDHs remain tetrameric
-
additional information
Q81W29
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
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IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
IMPDH is a homotetramer with square-planar symmetry. The four active sites are located near the subunit interfaces. The IMP site is contained within a monomer, and the residues that contact IMP are strongly conserved among all IMPDHs
additional information
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IMPDH is a homotetramer with square-planar symmetry. The four active sites are located near the subunit interfaces. The IMP site is contained within a monomer, and the residues that contact IMP are strongly conserved among all IMPDHs
additional information
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IMPDH is a homotetramer with square-planar symmetry. The four active sites are located near the subunit interfaces. The IMP site is contained within a monomer, and the residues that contact IMP are strongly conserved among all IMPDHs
-
additional information
the core of the catalytic domain comprises a (beta/alpha)8 barrel which represents the typical triose-phosphate isomerase fold (TIM barrel)
additional information
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the core of the catalytic domain comprises a (beta/alpha)8 barrel which represents the typical triose-phosphate isomerase fold (TIM barrel)
additional information
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the core of the catalytic domain comprises a (beta/alpha)8 barrel which represents the typical triose-phosphate isomerase fold (TIM barrel)
-
additional information
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the C-terminal extension unique to the retinal isoforms of IMPDH blocks the nucleic acid binding site
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
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IMPDH associates tightly with glycosomal protein sorting receptor PEX5
additional information
MtIMPDH predominates as a tetramer
additional information
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MtIMPDH predominates as a tetramer
-
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
IMPDHs share a two-domain organization composed of a catalytic domain and a smaller flanking domain containing two CBS motifs
additional information
-
IMPDHs share a two-domain organization composed of a catalytic domain and a smaller flanking domain containing two CBS motifs
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-