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Literature summary for 1.5.99.B2 extracted from

  • Sakuraba, H.; Satomura, T.; Kawakami, R.; Kim, K.; Hara, Y.; Yoneda, K.; Ohshima, T.
    Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix (2012), J. Biol. Chem., 287, 20070-20080.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.99.B2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) Codon Plus RILP cells Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme bound with L-proline, sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M trisodium citrate dihydrate (pH 5.6), and 30% (w/v) polyethylene glycol 4000 Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
 L-proline wild type enzyme, at pH 8.0 and 50°C Aeropyrum pernix
230
-
 L-proline DELTAL428 mutant enzyme, at pH 8.0 and 50°C Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
 2 * 18000 Aeropyrum pernix
36000
-
-
 Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-charged chelating Sepharose column chromatography and Sephacryl S-300 gel filtration Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + 2,6-dichlorophenolindophenol + H2O
-
 Aeropyrum pernix DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 18000 Aeropyrum pernix

Synonyms

Synonyms Comment Organism
L-proline dehydrogenase
-
 Aeropyrum pernix
LPDH
-
 Aeropyrum pernix

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Aeropyrum pernix