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Literature summary for 2.6.1.46 extracted from

  • Vandenende, C.S.; Vlasschaert, M.; Seah, S.Y.K.
    Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1 (2004), J. Bacteriol., 186, 5596-5602.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene pvdH, DNA sequence determination and analysis, subcloning and expression in Escherichia coli, overexpression in enzyme-knockout Pseudomonas aeruginosa strain PAO1 Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis, enzyme shows a ping-pong kinetic mechanism Pseudomonas aeruginosa
0.18
-
2-oxoglutarate pH 7.5, 25°C, recombinant enzyme Pseudomonas aeruginosa
0.26
-
L-2,4-diaminobutanoate pH 7.5, 25°C, with 2-oxoglutarate, recombinant enzyme Pseudomonas aeruginosa
0.29
-
L-2,4-diaminobutanoate pH 7.5, 25°C, with pyruvate, recombinant enzyme Pseudomonas aeruginosa
6.2
-
pyruvate pH 7.5, 25°C, recombinant enzyme Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
additional information iron-limiting conditions induce pyoverdine siderophore biosynthesis including enzyme activity Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
4 * 50000, recombinant enzyme, SDS-PAGE Pseudomonas aeruginosa
183000
-
recombinant enzyme, gel filtration Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa enzyme is involved in biosynthesis of the pyoverdine siderophore ?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
gene pvdH
-

Purification (Commentary)

Purification (Comment) Organism
221fold, recombinantly overexpressed enzyme from Pseudomonas aeruginosa strain PAO1 by anion exchange chromatography and gel filtration to 90% purity Pseudomonas aeruginosa

Reaction

Reaction Comment Organism Reaction ID
L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine ping-pong kinetic mechanism Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.21
-
purified recombinant enzyme, coupled assay with homoserine dehydrogenase from Saccharomyces cerevisiae Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2,4-diaminobutanoate + 2-oxoglutarate 2-oxoglutarate is the best amino donor substrate Pseudomonas aeruginosa L-aspartate 4-semialdehyde + L-glutamate
-
r
L-2,4-diaminobutanoate + pyruvate specificty for pyruvate is 41fold lower compared to 2-oxoglutarate Pseudomonas aeruginosa L-aspartate 4-semialdehyde + L-alanine
-
r
additional information enzyme is involved in biosynthesis of the pyoverdine siderophore Pseudomonas aeruginosa ?
-
?
additional information no activity with 2-oxobutyrate as amino acceptor Pseudomonas aeruginosa ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 50000, recombinant enzyme, SDS-PAGE Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas aeruginosa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.39
-
pyruvate pH 7.5, 25°C, recombinant enzyme Pseudomonas aeruginosa
1.39
-
2-oxoglutarate pH 7.5, 25°C, recombinant enzyme Pseudomonas aeruginosa

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Pseudomonas aeruginosa