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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

L-proline
+
a quinone
=
(S)-1-pyrroline-5-carboxylate
+
a quinol

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 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.99 With unknown physiological acceptors
                1.5.99.B2 proline dehydrogenase (acceptor)

Engineering

Engineering on EC 1.5.99.B2 - proline dehydrogenase (acceptor)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E64A
the mutation decreases the catalytic efficiency 27fold
G63A
the mutation decreases the catalytic efficiency 140fold
A167V
-
moderate reduction of POX activity
A455S
-
slight reduction of POX activity
A472T
-
slight reduction of POX activity
D426N
-
moderate reduction of POX activity
L289M
-
slight reduction of POX activity
L441P
-
severe reduction of POX activity
P460L
-
severe reduction of POX activity
Q19P
-
moderate reduction of POX activity
Q521E
-
severe reduction of POX activity
R185Q
-
slight reduction of POX activity
R185W
-
moderate reduction of POX activity
R431H
-
moderate reduction of POX activity
R453C
-
severe reduction of POX activity
T466M
-
severe reduction of POX activity
V427M
-
moderate reduction of POX activity
K110A
site-directed mutagenesis, inactive mutant
Y203F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K110A
-
site-directed mutagenesis, inactive mutant
-
Y203F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H225A
-
the mutant is unstable and precipitates from solution below pH 7.0, decreased activity compared to the wild type enzyme
H225Q
-
the mutant displays activity down to solution pH 6.0, increased activity compared to the wild type enzyme
Y251F
-
wild type pH stability, increased activity compared to the wild type enzyme
F10E/L12E
two point mutations in helix alphaA. This helix contains several hydrophobic residues. The recombinant MBP-tagged mutant variant exclusively forms tetramers and exhibits excellent catalytic features over a wide range of temperatures
additional information