1.5.5.2: proline dehydrogenase
This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.
Word Map on EC 1.5.5.2
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1.5.5.2
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putas
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schizophrenia
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pyrroline-5-carboxylate
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delta1-pyrroline-5-carboxylate
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flavoenzyme
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psycho
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hyperprolinemia
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microdeletion
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schizoaffective
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2-acetyl-1-pyrroline
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rgs4
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velocardiofacial
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proline-dependent
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digeorge
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dysbindin
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fragrant
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prolidase
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synthesis
- 1.5.5.2
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putas
-
schizophrenia
- pyrroline-5-carboxylate
- delta1-pyrroline-5-carboxylate
-
flavoenzyme
-
psycho
-
hyperprolinemia
-
microdeletion
-
schizoaffective
-
2-acetyl-1-pyrroline
- rgs4
-
velocardiofacial
-
proline-dependent
-
digeorge
-
dysbindin
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fragrant
- prolidase
- synthesis
Reaction
Synonyms
bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, EC 1.5.99.8, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH
ECTree
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Subunits
Subunits on EC 1.5.5.2 - proline dehydrogenase
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dimer
heterooctamer
4 * 55300 + 4 * 42700, calculated from amino acid sequence
octamer
tetramer
additional information
dimer
domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor
dimer
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE
dimer
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
dimer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
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tetramer
the enzyme is a alphabetagammadelta-type ProDH
tetramer
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE
homology-based three-dimensional structural modeling of JcProDH, overview
additional information
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homology-based three-dimensional structural modeling of JcProDH, overview
additional information
Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
additional information
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Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
additional information
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Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
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additional information
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
additional information
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recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
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