Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Glasser, N.R.; Wang, B.X.; Hoy, J.A.; Newman, D.K.
    The pyruvate and alpha-ketoglutarate dehydrogenase complexes of Pseudomonas aeruginosa catalyze pyocyanin and phenazine-1-carboxylic acid reduction via the subunit dihydrolipoamide dehydrogenase (2017), J. Biol. Chem., 292, 5593-5607 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 gene lpd3, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa
1.8.1.4 gene lpdG, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa
1.8.1.4 gene lpdV, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.4 purified enzyme in apoform, and in complexes with Nad+ and NADH, X-ray diffraction structure determination and analysis at 1.35-1.79 A resolution Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 I192G site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid Pseudomonas aeruginosa
1.8.1.4 V191Y site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.4 cyanide slight inhibition; slight inhibition; slight inhibition Pseudomonas aeruginosa
1.8.1.4 diphenyleneiodonium an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+ Pseudomonas aeruginosa
-
lipoamide + NADH + H+
-
r
1.8.1.4 dihydrolipoamide + NAD+ Pseudomonas aeruginosa UCBPP-PA14
-
lipoamide + NADH + H+
-
r
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ Pseudomonas aeruginosa by cell lysate reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ Pseudomonas aeruginosa UCBPP-PA14 by cell lysate reduced phenazine-1-carboxylic acid + NAD+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Pseudomonas aeruginosa A0A0H2Z9F5
-
-
1.8.1.4 Pseudomonas aeruginosa A0A0H2ZB32
-
-
1.8.1.4 Pseudomonas aeruginosa A0A0H2ZHZ0
-
-
1.8.1.4 Pseudomonas aeruginosa UCBPP-PA14 A0A0H2Z9F5
-
-
1.8.1.4 Pseudomonas aeruginosa UCBPP-PA14 A0A0H2ZB32
-
-
1.8.1.4 Pseudomonas aeruginosa UCBPP-PA14 A0A0H2ZHZ0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration Pseudomonas aeruginosa
1.8.1.4 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration. Purification of native pyruvate and2-oxoglutarate dehydrogenase complexes from strain PA14 by hydroxyapatite chromatography and gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
Pseudomonas aeruginosa lipoamide + NADH + H+
-
r
1.8.1.4 dihydrolipoamide + NAD+
-
Pseudomonas aeruginosa UCBPP-PA14 lipoamide + NADH + H+
-
r
1.8.1.4 methylene blue + NADH + H+
-
Pseudomonas aeruginosa reduced methylene blue + NAD+
-
?
1.8.1.4 methylene blue + NADH + H+
-
Pseudomonas aeruginosa UCBPP-PA14 reduced methylene blue + NAD+
-
?
1.8.1.4 additional information phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors Pseudomonas aeruginosa ?
-
?
1.8.1.4 additional information phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors Pseudomonas aeruginosa UCBPP-PA14 ?
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ by cell lysate Pseudomonas aeruginosa reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG Pseudomonas aeruginosa reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling Pseudomonas aeruginosa reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ by cell lysate Pseudomonas aeruginosa UCBPP-PA14 reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG Pseudomonas aeruginosa UCBPP-PA14 reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 phenazine-1-carboxylic acid + NADH + H+ the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling Pseudomonas aeruginosa UCBPP-PA14 reduced phenazine-1-carboxylic acid + NAD+
-
?
1.8.1.4 pyocyanin + NADH + H+ pyocyanin is reported to stimulate respiration Pseudomonas aeruginosa reduced pyocyanin + NAD+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 DLDH
-
Pseudomonas aeruginosa
1.8.1.4 Lpd3
-
Pseudomonas aeruginosa
1.8.1.4 LpdG
-
Pseudomonas aeruginosa
1.8.1.4 LpdV
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.4 28
-
assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 7.5
-
assay at Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
Pseudomonas aeruginosa
1.8.1.4 FAD binding structure analysis Pseudomonas aeruginosa
1.8.1.4 NAD+
-
Pseudomonas aeruginosa
1.8.1.4 NAD+ binding structure analysis Pseudomonas aeruginosa
1.8.1.4 NADH
-
Pseudomonas aeruginosa
1.8.1.4 NADH binding structure analysis Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.8.1.4 additional information purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful Pseudomonas aeruginosa
1.8.1.4 additional information purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview Pseudomonas aeruginosa
1.8.1.4 physiological function LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase Pseudomonas aeruginosa