1.5.5.2: proline dehydrogenase

This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.

Word Map on EC 1.5.5.2

Reaction

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

Synonyms

bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.5 With a quinone or similar compound as acceptor
                1.5.5.2 proline dehydrogenase

Engineering

Engineering on EC 1.5.5.2 - proline dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D370A
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 2.8fold lower than the ratio of the wild-type PutA86-601
D370A/Y540F
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 15fold lower than the ratio of the wild-type PutA86-601
L432P
mutant form of PutA86-669, 5fold decrease in turnover-number and a severe loss in thermostability
W194F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 50%
W194F/W211F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 95%
W211F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 80%
Y540A
-
a construct consisting of residue 86-630 of PutA is used
Y540F
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 5.8fold lower than the ratio of the wild-type PutA86-601
Y540S
-
a construct consisting of residue 86-630 of PutA is used
Y203F
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
F10E/L12E
additional information