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.
Word Map on EC 1.5.99.B2
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
1.5.99.B2 proline dehydrogenase (acceptor)Advanced search results
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results (KM Value
KM Value on EC 1.5.99.B2 - proline dehydrogenase (acceptor)
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
212.3
L-pipecolic acid
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
0.026
2,6-dichlorophenolindophenol
-
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
coenzyme Q1
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
L-proline
-
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
additional information
Michaelis-Menten and Haldane kinetics
-
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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