1.5.5.2: proline dehydrogenase

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

Reaction

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

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Results

in table

14060

AA Sequence

2

Application

1

CAS Registry Number

16

Cloned(Commentary)

25

Cofactor

6

Crystallization (Commentary)

140

Disease/ Diagnostics

19

Engineering

9

Expression

35

General Information

1

General Stability

36

Inhibitors

26

KCat/KM [mM/s]

10

Ki Value [mM]

33

KM Value [mM]

10

Localization

1

Metals/Ions

19

Molecular Weight [Da]

14

Natural Substrates/ Products (Substrates)

39

Organism

11

Pathway

55

PDB ID

13

pH Optimum

1

pH Range

2

pH Stability

1

pI Value

12

Purification (Commentary)

2

Reaction

3

Reaction Type

40

Reference

8

Source Tissue

9

Specific Activity [micromol/min/mg]

65

Substrates and Products (Substrate)

31

Subunits

84

Synonyms

1

Systematic Name

12

Temperature Optimum [°C]

1

Temperature Range [°C]

11

Temperature Stability [°C]

23

Turnover Number [1/s]

Reaction

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Reaction on EC 1.5.5.2 - proline dehydrogenase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

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

2 entries

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

switching of enzyme from a cytosolic DNA-binding protein to a membrane-bound enzyme involves W211 in a flexible domain near the proline dehydrogenase active site and occurs in a time scale 10fold lower than the turnover number

Escherichia coli

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671977

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

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