Information on EC 1.21.4.1 - D-proline reductase

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D-proline reductase (dithiol)

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EC 1.4.1.6

EC 1.4.4.1

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formerly

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lipoate-linked proline reductase

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PrdB

5-aminopentanoate + a [PrdC protein with a selenide-sulfide bridge] = D-proline + a [PrdC protein with thiol/selenol residues]

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oxidation

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redox reaction

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reduction

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reductive deamination

Arginine and proline metabolism, D-Amino acid metabolism

BRENDA

proline metabolism

KEGG

MetaCyc

L-proline degradation II (reductive Stickland reaction)

5-aminopentanoate:[PrdC protein] oxidoreductase (cyclizing)

A pyruvoyl- and L-selenocysteine-containing enzyme found in a number of Clostridial species. The pyruvoyl group, located on the PrdA subunit, binds the substrate, while the selenocysteine residue, located on the PrdB subunit, attacks the alpha-C-atom of D-proline, leading to a reductive cleavage of the C-N-bond of the pyrrolidine ring and formation of a selenoether. The selenoether is cleaved by a cysteine residue of PrdB, resulting in a mixed selenide-sulfide bridge, which is restored to its reduced state by another selenocysteine protein, PrdC. 5-aminopentanoate is released from PrdA by hydrolysis, regenerating the pyruvoyl moiety. The resulting mixed selenide-sulfide bridge in PrdC is reduced by NADH.

37255-43-9

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D-allohydroxyproline + dihydrolipoate

5-amino-4-hydroxypentanoic acid + lipoate

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Substrates: barely detectable activity
Products: -

ir

D-proline + 1,3-dimercaptopropanol

5-aminopentanoic acid + ?

D-proline + 6,8-dimercaptooctanoate

5-aminopentanoic acid + ?

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Substrates: -
Products: -

ir

D-proline + beta-mercaptoethanol

?

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Substrates: -
Products: -

ir

D-proline + dihydrolipoate

delta-aminovaleric acid + lipoate

D-proline + dithiol (reduced)

5-aminopentanoic acid + oxidized dithiol

3 entries

D-proline + dithiothreitol

5-amino pentanoic acid + ?

5 entries

D-proline + DL-lipoic acid

5-aminopentanoic acid + ?

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Substrates: -
Products: -

ir

D-proline + NADH

5-aminopentanoic acid + NAD+

4 entries

D-proline + NADH + H+

5-aminovalerate + NAD+

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Substrates: -
Products: -

r

D-proline + NADH

5-aminopentanoic acid + NAD+

4 entries

D-proline + NADH + H+

5-aminovalerate + NAD+

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Substrates: -
Products: -

r

NADH

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normal physiological electron donor in vivo, highly specific, NADPH is inactive as electron donor

484929, 484930

Ca2+

K+

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KF

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40 mM, maximal activity

Mg2+

3 entries

MgCl2

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40 mM, maximal activity

Mn2+

Na+

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Se2+

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containing selenium in form of selenocysteine and a carbonyl moiety, most probably a pyruvoyl group

2-Bromobutyrate

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2-Bromopropionate

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3-Bromopropionate

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alkaline phosphomonoesterase

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preparation from calf intestine, causes extensive inactivation

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arsenite

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Bromoacetate

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Co2+

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Delta-Aminovalerate

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Fe2+

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human seminal plasma

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50% inactivation by incubation at pH 5.5 for 90 min

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hydroxylamine

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Hydroxylamine hydrochloride

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iodoacetamide

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iodoacetate

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NaBH4

phenylhydrazine

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phenylhydrazine hydrochloride

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Sodium borohydride

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NAD+

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NH4+

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pyruvate

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covalently bound

thiol

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most effective activator towards iodoacetate inhibition

Tris

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0.26

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484929, 484933

16.1

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2.7

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2.71

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20.4

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8

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484931

Acetoanaerobium sticklandii DSM 519

4 entries

strain HF, DSM 517 T

Clostridioides difficile 630

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Clostridioides difficile

selenium-containing subunit PrdB

727777

Q17ZY6

UniProt

selenium-containing subunit PrdB

727777

Q17ZY6

UniProt

Clostridium sporogenes

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Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

metabolism

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catalyzes step 9 in the ornithine fermentation pathway

physiological function

23000

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10 * 23000 + 10 * 26000+ 10 * 45000, SDS-PAGE, mass spectrometry

484934, 484935

298000

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sedimentation equilibrium centrifugation

484929

30000

300000

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gel filtration

31000

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10 * 31000, adjusted for the weight of water molecules lost as a result of peptide bond cleavage

484929

327000

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gel filtration

484929

45000

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10 * 23000 + 10 * 26000+ 10 * 45000, SDS-PAGE, mass spectrometry

484934, 484935

870000

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gel filtration, native PAGE

decamer

7 entries

8.6

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maximum stability

484928

stability is greatly enhanced by polyvalent ions such as SO42- or HPO42-

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withstands ethanol and acetone fractionation at -20°C, does not lose activity as a result of prolonged dialysis

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Acetone

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withstands fractionation at -20°C, does not lose activity as a result of prolonged dialysis

Ethanol

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withstands fractionation at -20°C, does not lose activity as a result of prolonged dialysis

0-5°C purified enzyme stable for at least 1 month

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0°C frozen cells maintains essentially full enzyme activity for at least 4 months

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0°C frozen in solution retains constant enzyme activity for at least a week

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-

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2121, 484928, 484929, 484930, 484931, 484932, 484933, 484934, 484935

partially

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cloning of the genes encoding D-proline reductase, 4.8 kb EcoRI fragment containing the genes prdA and prdB isolated and sequenced, prdAcodes for a 68 kDa protein, posttranslationally cleaved to the 45 kDa and 23 kDa subunits, prdB encodes the 26 kDa subunit

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484934, 484935

D-proline reductase proproteins cloned and overexpressed in Escherichia coli XL2 blue and BL21

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484935

presence of proline activates transcription of the prd operon encoding D-proline reductase. Protein PrdR activates transcription of the poline reductase-encoding genes in the presence of proline