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acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
L-ornithine + N-acetyl-L-glutamate
N2-acetyl-L-ornithine + L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
N2-butyryl-L-ornithine + H2O
L-ornithine + butyric acid
-
-
-
-
?
N2-propionyl-L-ornithine + glutamate
L-ornithine + N-propionylglutamate
-
-
-
-
?
additional information
?
-
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
-
hydrolytic activity is 1% of the transferase activity
-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
specific for L-glutamate and L-ornithine
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
CLGAT can effectively participate in the biosynthesis of citrulline in leaves of during drought/strong-light stress
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
specific for L-glutamate
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
step in clavulanic acid biosynthesis via formation of arginine
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
additional information
?
-
OATase activity is measured using a ninhydrin procedure
-
-
-
additional information
?
-
-
OATase activity is measured using a ninhydrin procedure
-
-
-
additional information
?
-
OATase activity is measured using a ninhydrin procedure
-
-
-
additional information
?
-
enzyme also shows low hydrolase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
CLGAT can effectively participate in the biosynthesis of citrulline in leaves of during drought/strong-light stress
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
step in clavulanic acid biosynthesis via formation of arginine
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
evolution
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
evolution
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
evolution
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
malfunction
inactivation of argJ does not cause arginine auxotrophy or marked growth defects
malfunction
enzyme inhibitor pranlukast (PRK) treatment remarkably abates the survival of free as well as macrophage-internalized Mtb, and shows enhanced efficacy in combination with standard-of-care drugs. Notably, PRK also reduces the 5-lipoxygenase (5-LO) signaling in the infected macrophages, thereby surmounting an enhanced response against intracellular pathogen. Further, treatment with PRK alone or with rifampicin leads to significant decrease in Mycobacterium tuberculosis burden and tubercular granulomas in Mtb-infected mice lungs. PRK-mediated killing of Mycobacterium tuberculosis is rescued upon arginine supplementation
malfunction
-
enzyme inhibitor pranlukast (PRK) treatment remarkably abates the survival of free as well as macrophage-internalized Mtb, and shows enhanced efficacy in combination with standard-of-care drugs. Notably, PRK also reduces the 5-lipoxygenase (5-LO) signaling in the infected macrophages, thereby surmounting an enhanced response against intracellular pathogen. Further, treatment with PRK alone or with rifampicin leads to significant decrease in Mycobacterium tuberculosis burden and tubercular granulomas in Mtb-infected mice lungs. PRK-mediated killing of Mycobacterium tuberculosis is rescued upon arginine supplementation
-
malfunction
-
enzyme inhibitor pranlukast (PRK) treatment remarkably abates the survival of free as well as macrophage-internalized Mtb, and shows enhanced efficacy in combination with standard-of-care drugs. Notably, PRK also reduces the 5-lipoxygenase (5-LO) signaling in the infected macrophages, thereby surmounting an enhanced response against intracellular pathogen. Further, treatment with PRK alone or with rifampicin leads to significant decrease in Mycobacterium tuberculosis burden and tubercular granulomas in Mtb-infected mice lungs. PRK-mediated killing of Mycobacterium tuberculosis is rescued upon arginine supplementation
-
metabolism
overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production
metabolism
ArgJ plays a vital role in the L-citrulline biosynthesis. The enzyme exerts feedback inhibition on N-acetylglutamate synthase, pathway overview
metabolism
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
metabolism
the enzyme is involved in the arginine biosynthetic pathway
metabolism
the L-ornithine biosynthetic pathway is cyclic due to L-ornithine acetyltransferase (OATase), which catalyzes the conversion of N-acetyl-L-ornithine and L-glutamate to L-ornithine and N-acetyl-Lglutamate (NAG). NAG kinase (NAGK, encoded by argB, EC 2.7.2.8) then phosphorylates NAG in the second step of the pathway. In addition to OATase and NAGK, argC-encoded N-acetyl-L-glutamate 5-semialdehyde dehydrogenase, and argD-encoded N-acetyl-L-ornithine aminotransferase are critical for the conversion of L-glutamate to L-ornithine. These four genes are generally involved in one of the L-arginine synthesis clusters, named argCJBD in Corynebacterium strains
metabolism
-
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
-
metabolism
-
the L-ornithine biosynthetic pathway is cyclic due to L-ornithine acetyltransferase (OATase), which catalyzes the conversion of N-acetyl-L-ornithine and L-glutamate to L-ornithine and N-acetyl-Lglutamate (NAG). NAG kinase (NAGK, encoded by argB, EC 2.7.2.8) then phosphorylates NAG in the second step of the pathway. In addition to OATase and NAGK, argC-encoded N-acetyl-L-glutamate 5-semialdehyde dehydrogenase, and argD-encoded N-acetyl-L-ornithine aminotransferase are critical for the conversion of L-glutamate to L-ornithine. These four genes are generally involved in one of the L-arginine synthesis clusters, named argCJBD in Corynebacterium strains
-
metabolism
-
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
-
metabolism
-
ArgJ plays a vital role in the L-citrulline biosynthesis. The enzyme exerts feedback inhibition on N-acetylglutamate synthase, pathway overview
-
metabolism
-
the enzyme is involved in the arginine biosynthetic pathway
-
metabolism
-
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
-
metabolism
-
the enzyme is involved in the arginine biosynthetic pathway
-
metabolism
-
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
-
metabolism
-
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
-
physiological function
ArgJ in Mycobacterium tuberculosis is a monofunctional enzyme as it facilitates the transfer of acetyl group to glutamate exclusively from N-acetyl ornithine
physiological function
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
physiological function
-
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
-
physiological function
-
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
-
physiological function
-
ArgJ in Mycobacterium tuberculosis is a monofunctional enzyme as it facilitates the transfer of acetyl group to glutamate exclusively from N-acetyl ornithine
-
physiological function
-
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
-
physiological function
-
ArgJ in Mycobacterium tuberculosis is a monofunctional enzyme as it facilitates the transfer of acetyl group to glutamate exclusively from N-acetyl ornithine
-
physiological function
-
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
-
physiological function
-
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
-
additional information
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-l-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, lacking a functional ArgJ, to mimic the linear pathway of L-ornithine biosynthesis
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-l-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, lacking a functional ArgJ, to mimic the linear pathway of L-ornithine biosynthesis
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-l-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, lacking a functional ArgJ, to mimic the linear pathway of L-ornithine biosynthesis
-
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proteolytic modification
-
the two subunits withj molecular masses of 21300 Da and 23500 Da are derived from a single precursor polypeptide, suggesting that the CLGAT precursor is cleaved autocatalytically at the conserved ATML motif. The first 26-amino acid sequence at the N-terminus of the precursor functions as a chloroplast transit peptide
proteolytic modification
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
-
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
-
proteolytic modification
enzyme MtArgJ belongs to the N-terminal nucleophile (Ntn) fold class of enzymes, synthesized as a 404-amino acid long protein, which undergoes an autoproteolysis event between the Ala199 and Thr200. This autoproteolysis generates two fragments of approximately equal size (20-21 kDa), which then associate to form a protomeric unit (AB-heterodimer; A2B2 tetramer-dimer of the heterodimer)
proteolytic modification
-
enzyme MtArgJ belongs to the N-terminal nucleophile (Ntn) fold class of enzymes, synthesized as a 404-amino acid long protein, which undergoes an autoproteolysis event between the Ala199 and Thr200. This autoproteolysis generates two fragments of approximately equal size (20-21 kDa), which then associate to form a protomeric unit (AB-heterodimer; A2B2 tetramer-dimer of the heterodimer)
-
proteolytic modification
-
enzyme MtArgJ belongs to the N-terminal nucleophile (Ntn) fold class of enzymes, synthesized as a 404-amino acid long protein, which undergoes an autoproteolysis event between the Ala199 and Thr200. This autoproteolysis generates two fragments of approximately equal size (20-21 kDa), which then associate to form a protomeric unit (AB-heterodimer; A2B2 tetramer-dimer of the heterodimer)
-
proteolytic modification
autoproteolysis occurs between A194/T195, which results in generation of alpha and beta polypeptides
proteolytic modification
enzyme belongs to the N-terminal nucleophile hydrolase class of self-processing acetyltransferases
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E354A
-
change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
F121C
-
change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
G360P
-
change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
G362S
-
change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
D150G
autoprocessing to alpha-,beta-subunits: 50% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 50% (wild-type 100%)
DELTA1389
autoprocessing to alpha-,beta-subunits: 100% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
E260A
autoprocessing to alpha-,beta-subunits: not determined (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
K170A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 5% (wild-type 100%)
T148A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 2% (wild-type: 100%)
T149A
autoprocessing to alpha-,beta-subunits: 80% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 10% (wild-type: 100%)
E280A
-
change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
F35C
-
change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation leads to partial inhibition of both synthase and kinase activities by arginine and decrease in synthase activity
G286P
-
change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
G288S
-
change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine inhibition and decreases synthase activity
additional information
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
-
additional information
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
-
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
-
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
-
additional information
-
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
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Morris, C.J.; Thompson, J.F.
Acetyl coenzyme A-glutamate acetyltransferase and N2-acetylornithine-glutamate acetyltransferase of Chlorella
Plant Physiol.
55
960-967
1975
Chlorella vulgaris
brenda
Jain, J.C.; Shargool, P.D.
A modified assay system for enzymes involved in N-acetyl group transfer reactions: its use to study enzymes involved in ornithine biosynthesis in plants
Anal. Biochem.
138
25-29
1984
Pisum sativum
brenda
Staub, M.; Denes, G.
Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I. Purification and properties of ornithine acetyltransferase
Biochim. Biophys. Acta
128
82-91
1966
Chlamydomonas reinhardtii
brenda
Meile, L.; Leisinger, T.
Enzymes of arginine biosynthesis in methanogenic bacteria
Experientia
40
899-900
1984
Methanothermobacter thermautotrophicus, Methanobrevibacter arboriphilus, Methanococcus vannielii
-
brenda
Kershaw, N.J.; McNaughton, H.J.; Hewitson, K.S.; Hernandez, H.; Griffin, J.; Hughes, C.; Greaves, P.; Barton, B.; Robinson, C.V.; Schofield, C.J.
ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity
Eur. J. Biochem.
269
2052-2059
2002
Streptomyces clavuligerus
brenda
Liu, Y.; Van Heeswijck, R.; Hoj, P.; Hoogenraad, N.
Purification and characterization of ornithine acetyltransferase from Saccharomyces cerevisiae
Eur. J. Biochem.
228
291-296
1995
Saccharomyces cerevisiae
brenda
Marc, F.; Weigel, P.; Legrain, C.; Almeras, Y.; Santrot, M.; Glansdorff, N.; Sakanyan, V.
Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms
Eur. J. Biochem.
267
5217-5226
2000
Geobacillus stearothermophilus, Methanocaldococcus jannaschii, Thermotoga neapolitana
brenda
Crabeel, M.; Abadjieva, A.; Hilven, P.; Desimpelaere, J.; Soetens, O.
Characterization of the Saccharomyces cerevisiae ARG7 gene encoding ornithine acetyltransferase, an enzyme also endowed with acetylglutamate synthase activity
Eur. J. Biochem.
250
232-241
1997
Saccharomyces cerevisiae
brenda
Sakanyan, V.; Charlier, D.; Legrain, C.; Kochikyan, A.; Mett, I.; Pierard, A.; Glansdorff, N.
Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase
J. Gen. Microbiol.
139
393-402
1993
Geobacillus stearothermophilus
brenda
Marc, F.; Weigel, P.; Legrain, C.; Glansdorff, N.; Sakanyan, V.
An invariant threonine is involved in self-catalyzed cleavage of the precursor protein for ornithine acetyltransferase
J. Biol. Chem.
276
25404-25410
2001
Geobacillus stearothermophilus
brenda
Abadjieva, A.; Hilven, P.; Pauwels, K.; Crabeel, M.
The yeast ARG7 gene product is autoproteolyzed to two subunit peptides, yielding active ornithine acetyltransferase
J. Biol. Chem.
275
11361-11367
2000
Saccharomyces cerevisiae
brenda
Elkins, J.M.; Kershaw, N.J.; Schofield, C.J.
X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster
Biochem. J.
385
565-573
2005
Streptomyces clavuligerus (P0DJQ5)
brenda
Cheng, H.; Grishin, N.V.
DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain
Protein Sci.
14
1902-1910
2005
Streptomyces clavuligerus
brenda
Maes, D.; Crabeel, M.; Van De Weerdt, C.; Martial, J.; Peeters, E.; Charlier, D.; Decanniere, K.; Vanhee, C.; Wyns, L.; Zegers, I.
Crystallization of ornithine acetyltransferase from yeast by counter-diffusion and preliminary X-ray study
Acta Crystallogr. Sect. F
F62
1294-1297
2006
Saccharomyces cerevisiae
brenda
Takahara, K.; Akashi, K.; Yokota, A.
Purification and characterization of glutamate N-acetyltransferase involved in citrulline accumulation in wild watermelon
FEBS J.
272
5353-5364
2005
Citrullus lanatus
brenda
Haskins, N.; Panglao, M.; Qu, Q.; Majumdar, H.; Cabrera-Luque, J.; Morizono, H.; Tuchman, M.; Caldovic, L.
Inversion of allosteric effect of arginine on N-acetylglutamate synthase, a molecular marker for evolution of tetrapods
BMC Biochem.
9
24
2008
Mus musculus, Xanthomonas campestris
brenda
Sankaranarayanan, R.; Garen, C.R.; Cherney, M.M.; Yuan, M.; Lee, C.; James, M.N.
Preliminary X-ray crystallographic analysis of ornithine acetyltransferase (Rv1653) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
65
173-176
2009
Mycobacterium tuberculosis (P9WPZ3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPZ3)
brenda
Iqbal, A.; Clifton, I.J.; Bagonis, M.; Kershaw, N.J.; Domene, C.; Claridge, T.D.; Wharton, C.W.; Schofield, C.J.
Anatomy of a simple acyl intermediate in enzyme catalysis: combined biophysical and modeling studies on ornithine acetyl transferase
J. Am. Chem. Soc.
131
749-757
2009
Streptomyces clavuligerus (P0DJQ5)
brenda
Dou, W.; Xu, M.; Cai, D.; Zhang, X.; Rao, Z.; Xu, Z.
Improvement of L-arginine production by overexpression of a bifunctional ornithine acetyltransferase in Corynebacterium crenatum
Appl. Biochem. Biotechnol.
165
845-855
2011
Corynebacterium crenatum (C1KGU6), Corynebacterium crenatum
brenda
Sankaranarayanan, R.; Cherney, M.M.; Garen, C.; Garen, G.; Niu, C.; Yuan, M.; James, M.N.
The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor
J. Mol. Biol.
397
979-990
2010
Mycobacterium tuberculosis (P9WPZ3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPZ3)
brenda
Iqbal, A.; Clifton, I.J.; Chowdhury, R.; Ivison, D.; Domene, C.; Schofield, C.J.
Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates
Org. Biomol. Chem.
9
6219-6225
2011
Streptomyces clavuligerus (P0DJQ5)
brenda
Van de Casteele, M.; Demarez, M.; Legrain, C.; Glansdorff, N.; Pierard, A.
Pathways of arginine biosynthesis in extreme thermophilic archaeo- and eubacteria
J. Gen. Microbiol.
136
1177-1183
1990
no activity in Sulfolobus solfataricus
-
brenda
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Shen, P.; Yan, M.; Li, Y.; Xu, L.
Implication of ornithine acetyltransferase activity on L-ornithine production in Corynebacterium glutamicum
Biotechnol. Appl. Biochem.
63
15-21
2016
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q59280)
brenda
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Yan, M.; Li, Y.; Guo, K.; Xu, L.
Improvement of L-citrulline production in Corynebacterium glutamicum by ornithine acetyltransferase
J. Ind. Microbiol. Biotechnol.
42
307-313
2015
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q59280), Corynebacterium glutamicum ATCC 13032
brenda
Hernandez, V.M.; Girard, L.; Hernandez-Lucas, I.; Vazquez, A.; Ortiz-Ortiz, C.; Diaz, R.; Dunn, M.F.
Genetic and biochemical characterization of arginine biosynthesis in Sinorhizobium meliloti 1021
Microbiology
161
1671-1682
2015
Sinorhizobium meliloti (Q92MJ1), Sinorhizobium meliloti
brenda
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Shen, P.; Yan, M.; Li, Y.; Xu, L.
Implication of ornithine acetyltransferase activity on L-ornithine production in Corynebacterium glutamicum
Biotechnol. Appl. Biochem.
63
15-21
2016
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum LMG 3730 (Q59280), Corynebacterium glutamicum ATCC 13032 (Q59280), Corynebacterium glutamicum JCM 1318 (Q59280), Corynebacterium glutamicum NCIMB 10025 (Q59280), Corynebacterium glutamicum DSM 20300 (Q59280)
brenda
Mishra, A.; Mamidi, A.S.; Rajmani, R.S.; Ray, A.; Roy, R.; Surolia, A.
An allosteric inhibitor of Mycobacterium tuberculosis ArgJ implications to a novel combinatorial therapy
EMBO Mol. Med.
10
e8038
2018
Mycobacterium tuberculosis (P9WPZ3), Mycobacterium tuberculosis H37Rv (P9WPZ3), Mycobacterium tuberculosis ATCC 25618 (P9WPZ3)
brenda
Shu, Q.; Xu, M.; Li, J.; Yang, T.; Zhang, X.; Xu, Z.; Rao, Z.
Improved L-ornithine production in Corynebacterium crenatum by introducing an artificial linear transacetylation pathway
J. Ind. Microbiol. Biotechnol.
45
393-404
2018
no activity in Escherichia coli, Corynebacterium crenatum (P62058), Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5 (P62058)
brenda