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Information on EC 2.6.1.84 - arginine-pyruvate transaminase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HUI9
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2.6.1.84 arginine-pyruvate transaminaseIUBMB Comments
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.
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aruf mutant, arginine:pyruvate transaminase, arginine/lysine:pyruvate transaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
ping-pong kinetic mechanism
-
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
aruF mutant with inducible L-arginine:pyruvate transaminase activity
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
AruH catalyzes the first step of the arginine transaminase pathway, representing one of the multiple pathways for L-arginine catabolism
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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
52660-17-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamine + pyruvate
2-oxoglutaramate + L-alanine
-
broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
-
-
?
L-lysine + pyruvate
DELTA1-piperideine-2-carboxylate + L-alanine
-
-
product identification by mass spectrometry
-
?
L-lysine + pyruvate
DELTA1-piperidine-2-carboxylate + L-alanine
-
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
-
?
L-methionine + pyruvate
4-methylthio-2-oxo-butanoate + L-alanine
-
-
-
-
?
L-methionine + pyruvate
4-methylthio-2-oxobutanoate + L-alanine
-
broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
-
-
?
L-ornithine + pyruvate
5-amino-2-oxopentanoate + L-alanine
-
broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
-
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
-
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
-
product identification by mass spectrometry
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
AruH catalyzes the first step of the arginine transaminase pathway, representing one of the multiple pathways for L-arginine catabolism
-
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
detected by HPLC and mass spectrometry
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
AruH catalyzes the first step in the arginine transaminase pathway, converting the substrates L-arginine and pyruvate into 2-ketoarginine and L-alanine, AruH may have a broader physiological function in amino acid catabolism
-
-
?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
broad substrate specificity, preference in decreasing order: L-arginine, L-lysine, L-methionine, L-leucine, L-ornithine, L-glutamine
-
-
?
additional information
?
-
-
knockout of aruH and aruI, which encode an arginine:pyruvate transaminase and a 2-ketoarginine decarboxylase in an operon, also abolishes the ability of the aruF mutant to grow on L-arginine
-
-
?
additional information
?
-
knockout of aruH and aruI, which encode an arginine:pyruvate transaminase and a 2-ketoarginine decarboxylase in an operon, also abolishes the ability of the aruF mutant to grow on L-arginine
-
-
?
additional information
?
-
-
arginine utilization proceeds via multiple catabolic pathways in the organism, the enzyme is involved in the arginine transaminase pathway, regulation of arginine-responsive induction of the arginine transaminase pathway, arginine metabolism, overview
-
-
?
additional information
?
-
arginine utilization proceeds via multiple catabolic pathways in the organism, the enzyme is involved in the arginine transaminase pathway, regulation of arginine-responsive induction of the arginine transaminase pathway, arginine metabolism, overview
-
-
?
additional information
?
-
AruH is also an L-ATase, overview
-
-
?
additional information
?
-
-
broad substrate specificity in an descending order of preference: Arg, Lys, Met, Leu, Orn, Gln
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
AruH catalyzes the first step of the arginine transaminase pathway, representing one of the multiple pathways for L-arginine catabolism
-
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
AruH catalyzes the first step in the arginine transaminase pathway, converting the substrates L-arginine and pyruvate into 2-ketoarginine and L-alanine, AruH may have a broader physiological function in amino acid catabolism
-
-
?
additional information
?
-
-
knockout of aruH and aruI, which encode an arginine:pyruvate transaminase and a 2-ketoarginine decarboxylase in an operon, also abolishes the ability of the aruF mutant to grow on L-arginine
-
-
?
additional information
?
-
knockout of aruH and aruI, which encode an arginine:pyruvate transaminase and a 2-ketoarginine decarboxylase in an operon, also abolishes the ability of the aruF mutant to grow on L-arginine
-
-
?
additional information
?
-
-
arginine utilization proceeds via multiple catabolic pathways in the organism, the enzyme is involved in the arginine transaminase pathway, regulation of arginine-responsive induction of the arginine transaminase pathway, arginine metabolism, overview
-
-
?
additional information
?
-
arginine utilization proceeds via multiple catabolic pathways in the organism, the enzyme is involved in the arginine transaminase pathway, regulation of arginine-responsive induction of the arginine transaminase pathway, arginine metabolism, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
13.9
L-arginine
-
pH 9.0, 37°C, coupled reaction with NAD+ and L-alanine dehydrogenase
1.6
pyruvate
-
pH 9.0, 37°C, coupled reaction with NAD+ and L-alanine dehydrogenase
additional information
additional information
-
catalytic efficiency kcat/KM 24.1 mM/s for pyruvate and 2.8 mM/s for arginine
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
38.6
pyruvate
-
calculated, pH 9.0, 37°C, coupled reaction with NAD+ and L-alanine dehydrogenase
additional information
additional information
-
catalytic efficiency kcat/KM 24.1 mM/s for pyruvate and 2.8 mM/s for arginine
-
38.6
L-arginine
-
calculated, pH 9.0, 37°C, coupled reaction with NAD+ and L-alanine dehydrogenase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a coupled reaction assay with NAD+ and L-alanine dehydrogenase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 42
-
the enzyme is prone to sharp thermal inactivation above this temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
79300
79300
-
native enzyme, gel filtration, apparent mass, indicating that His-tagged AruH is a homodimer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of the PA4976 aruH knockout mutant
additional information
construction of the PA4976 aruH knockout mutant
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aruH, overexpression of soluble His-tagged enzyme in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, Z.; Lu, C.D.
Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa
J. Bacteriol.
189
3945-3953
2007
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HUI9), Pseudomonas aeruginosa PAO4558
Yang, Z.; Lu, C.D.
Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1
J. Bacteriol.
189
3954-3959
2007
Pseudomonas aeruginosa
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