Information on EC 2.6.1.84 - arginine-pyruvate transaminase

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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

EC NUMBER
COMMENTARY hide
2.6.1.84
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RECOMMENDED NAME
GeneOntology No.
arginine-pyruvate transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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L-arginine degradation IX (arginine:pyruvate transaminase pathway)
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Metabolic pathways
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arginine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-arginine:pyruvate aminotransferase
A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked.
CAS REGISTRY NUMBER
COMMENTARY hide
52660-17-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PAO4558
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
L-glutamine + pyruvate
2-oxoglutaramate + L-alanine
show the reaction diagram
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broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
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?
L-glutamine + pyruvate
?
show the reaction diagram
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-
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?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
show the reaction diagram
L-lysine + pyruvate
DELTA1-piperideine-2-carboxylate + L-alanine
show the reaction diagram
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product identification by mass spectrometry
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?
L-lysine + pyruvate
DELTA1-piperidine-2-carboxylate + L-alanine
show the reaction diagram
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broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
mass spectrometry analysis, implies that AruH may have broader physiological functions in amino acid catabolism
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?
L-methionine + pyruvate
4-methylthio-2-oxo-butanoate + L-alanine
show the reaction diagram
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?
L-methionine + pyruvate
4-methylthio-2-oxobutanoate + L-alanine
show the reaction diagram
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broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
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-
?
L-ornithine + pyruvate
5-amino-2-oxopentanoate + L-alanine
show the reaction diagram
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broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
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?
L-ornithine + pyruvate
?
show the reaction diagram
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?
additional information
?
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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
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
borate/NaOH buffer
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strong inhibition at pH 9.0
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
induces the L-ATase activity at least 76fold in an aruF mutant strain, but not in the wild-type strain PAO1
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 13.9
L-arginine
1.6
pyruvate
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pH 9.0, 37C; pH 9.0, 37C, coupled reaction with NAD+ and L-alanine dehydrogenase
additional information
additional information
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catalytic efficiency kcat/KM 24.1 mM/s for pyruvate and 2.8 mM/s for arginine; kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.6
L-arginine
Pseudomonas aeruginosa
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calculated, pH 9.0, 37C, coupled reaction with NAD+ and L-alanine dehydrogenase; pH 9.0, 37C
38.6
pyruvate
Pseudomonas aeruginosa
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calculated, pH 9.0, 37C, coupled reaction with NAD+ and L-alanine dehydrogenase
additional information
additional information
Pseudomonas aeruginosa
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catalytic efficiency kcat/KM 24.1 mM/s for pyruvate and 2.8 mM/s for arginine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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; in borate/NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
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activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
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; sharp inactivation above
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 42
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the enzyme is prone to sharp thermal inactivation above this temperature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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2 * 43000, recombinant enzyme, SDS-PAGE; 2 * 43000, SDS-PAGE, His-tagged
79300
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native enzyme, gel filtration, apparent mass, indicating that His-tagged AruH is a homodimer; recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 43000, recombinant enzyme, SDS-PAGE
homodimer
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2 * 43000, SDS-PAGE, His-tagged
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, to homogeneity, using HisTrap HP kit, anion exchange chromatography Mono Q; recombinant His-tagged AruH from Escherichia coli to homogeneity by affinity and anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aruH or PA4976, location in the aruIH locus
gene aruH, overexpression of soluble His-tagged enzyme in Escherichia coli; overexpressed in Escherichia coli
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used in complementation experiments
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information