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Literature summary for 1.5.99.B2 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
Search for more literature for 1.5.99.B2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)pLysS cells Deinococcus radiodurans

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in the oxidized state complexed with the proline analogue L-tetrahydrofuroic acid and in the reduced state with the proline site vacant, sitting drop vapor diffusion method, using 0.2 M MgCl2, 25% (w/v) PEG 3350, and 0.1 mM Bis-Tris (pH 5.8), at 22°C Deinococcus radiodurans

Protein Variants

Protein Variants Comment Organism
E64A the mutation decreases the catalytic efficiency 27fold Deinococcus radiodurans
G63A the mutation decreases the catalytic efficiency 140fold Deinococcus radiodurans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
 coenzyme Q1 mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.032
-
 coenzyme Q1 mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.155
-
 coenzyme Q1 wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
50
-
 L-proline mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
290
-
 L-proline wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
384
-
 L-proline mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans Q9RW55
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Hitrap Q column chromatography Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + coenzyme Q1 + H2O
-
 Deinococcus radiodurans DELTA1-pyrroline-5-carboxylate + reduced coenzyme Q1
-
 ?

Synonyms

Synonyms Comment Organism
PRODH
-
 Deinococcus radiodurans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.043
-
 coenzyme Q1 mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.046
-
 coenzyme Q1 mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.055
-
 L-proline mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
0.08
-
 L-proline mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
8.7
-
 L-proline wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans
14
-
 coenzyme Q1 wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5) Deinococcus radiodurans

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Deinococcus radiodurans