1.5.99.B2: proline dehydrogenase (acceptor)
This is an abbreviated version!
For detailed information about proline dehydrogenase (acceptor), go to the full flat file.
Reaction
Synonyms
APE_1267.1, dye-linked L-proline dehydrogenase, L-proDH, L-proline dehydrogenase, L-proline: FAD oxidoreductase, L-proline:FAD oxidoreductase, LPDH, PDH, PDH1, PDH2, PF1246, PF1798, PH1364, PH1751, PIG6, POX, Pro dehydrogenase, PRODH, ProDH1, ProDH2, proline dehydrogenase, proline oxidase, prub, PutA, TK0117, TK0122, TPpdhB, TPpdhB2, TtProDH
ECTree
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KM Value
KM Value on EC 1.5.99.B2 - proline dehydrogenase (acceptor)
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212.3
L-pipecolic acid
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
0.026
-
with L-proline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
0.035
2,6-dichlorophenolindophenol
-
with L-hydroxyproline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
3.4
2,6-dichlorophenolindophenol
pH 7.1, 25°C, recombinant wild-type enzyme
0.028
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.032
coenzyme Q1
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.155
coenzyme Q1
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.174
-
PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
0.334
L-proline
-
PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
0.689
L-proline
-
PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
1.46
L-proline
-
TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
1.95
L-proline
-
mutant enzyme Y215F, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
2.38
L-proline
-
TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
2.46
L-proline
TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
2.5 - 5
L-proline
-
PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
3.5
L-proline
TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
5.3
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 50°C
5.6
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 40°C
6.5
L-proline
pH 7.4, 45°C, recombinant wild-type enzyme, Haldane kinetics
9.9
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
11.5
L-proline
pH 7.4, 25°C, recombinant wild-type enzyme, Michaelis-Menten kinetics
14.46
L-proline
-
mutant enzyme H225Q, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
16.5
L-proline
pH 7.4, 25°C, recombinant wild-type enzyme, Haldane kinetics
19.67
L-proline
-
mutant enzyme H225A, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
19.9
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 70°C
27
L-proline
with 2,6-dichlorophenolindophenol as cosubstrate, in 50 mM Tris-HCl, at 25°C
30.8
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
31
L-proline
-
in 100 mM TrisHCl, 10 mM MgCl2, 10% (v/v) glycerol, pH 8.5, at 25°C
33.8
L-proline
pH 7.4, 45°C, recombinant mutant F10E/L12E, Haldane kinetics
50
L-proline
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
67.6
L-proline
pH 7.4, 25°C, recombinant mutant F10E/L12E, Michaelis-Menten kinetics
175.1
L-proline
pH 7.4, 25°C, recombinant mutant F10E/L12E, Haldane kinetics
290
L-proline
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
384
L-proline
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
additional information
Michaelis-Menten and Haldane kinetics
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additional information
additional information
Michaelis-Menten kinetics, steady-state kinetics and pre-steady-state kinetics of wild-type and mutant enzymes, stopped-flow kinetic isotope effects, bisubstrate kinetic analysis, overview
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