Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.5.2 extracted from

  • Luo, M.; Arentson, B.W.; Srivastava, D.; Becker, D.F.; Tanner, J.J.
    Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release (2012), Biochemistry, 51, 10099-10108.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00021
-
L-proline mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.0011
-
L-proline mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.03
-
L-proline wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
1.438
-
coenzyme Q1 mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
1.535
-
coenzyme Q1 mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
90.32
-
coenzyme Q1 wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans