Information on EC 1.21.4.1 - D-proline reductase (dithiol)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.21.4.1
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RECOMMENDED NAME
GeneOntology No.
D-proline reductase (dithiol)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-aminopentanoate + lipoate = D-proline + dihydrolipoate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
-
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reductive deamination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-aminopentanoate:lipoate oxidoreductase (cyclizing)
The reaction is observed only in the direction of D-proline reduction. Other dithiols can function as reducing agents; the enzyme contains a pyruvoyl group and a selenocysteine residue, both essential for activity.
CAS REGISTRY NUMBER
COMMENTARY hide
37255-43-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
selenium-containing subunit PrdB
UniProt
Manually annotated by BRENDA team
selenium-containing subunit PrdB
UniProt
Manually annotated by BRENDA team
strain HF, DSM 517 T
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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catalyzes step 9 in the ornithine fermentation pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-allohydroxyproline + dihydrolipoate
5-amino-4-hydroxypentanoic acid + lipoate
show the reaction diagram
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barely detectable activity
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ir
D-proline + 1,3-dimercaptopropanol
5-aminopentanoic acid + ?
show the reaction diagram
D-proline + 6,8-dimercaptooctanoate
5-aminopentanoic acid + ?
show the reaction diagram
-
-
-
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ir
D-proline + beta-mercaptoethanol
?
show the reaction diagram
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-
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ir
D-proline + dihydrolipoate
delta-aminovaleric acid + lipoate
show the reaction diagram
D-proline + dithiol (reduced)
5-aminopentanoic acid + oxidized dithiol
show the reaction diagram
D-proline + dithiothreitol
5-amino pentanoic acid + ?
show the reaction diagram
D-proline + DL-lipoic acid
5-aminopentanoic acid + ?
show the reaction diagram
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ir
D-proline + NADH
5-aminopentanoic acid + NAD+
show the reaction diagram
D-proline + NADH + H+
5-aminovalerate + NAD+
show the reaction diagram
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r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-proline + NADH
5-aminopentanoic acid + NAD+
show the reaction diagram
D-proline + NADH + H+
5-aminovalerate + NAD+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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normal physiological electron donor in vivo, highly specific, NADPH is inactive as electron donor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KF
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40 mM, maximal activity
MgCl2
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40 mM, maximal activity
Se2+
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containing selenium in form of selenocysteine and a carbonyl moiety, most probably a pyruvoyl group
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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Bromoacetate
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Delta-Aminovalerate
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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 hydrochloride
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NaBH4
phenylhydrazine
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phenylhydrazine hydrochloride
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Sodium borohydride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyruvate
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covalently bound
thiol
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most effective activator towards iodoacetate inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
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10 * 23000 + 10 * 26000+ 10 * 45000, SDS-PAGE, mass spectrometry
31000
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10 * 31000, adjusted for the weight of water molecules lost as a result of peptide bond cleavage
45000
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10 * 23000 + 10 * 26000+ 10 * 45000, SDS-PAGE, mass spectrometry
298000
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sedimentation equilibrium centrifugation
300000
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gel filtration
327000
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gel filtration
870000
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gel filtration, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
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maximum stability
484928
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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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; D-proline reductase proproteins cloned and overexpressed in Escherichia coli XL2 blue and BL21
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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