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3'-hydroxymethylcephem + carbamoyl phosphate
cephamycin C + phosphate
arsenate + L-citrulline
carbamoylarsenate + L-ornithine
-
pseudo-reverse reaction, arsenate is first coupled to citrulline, followed by elimination of carbamoylarsenate
-
r
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
carbamoyl phosphate + diaminobutane
phosphate + ?
-
-
-
-
?
carbamoyl phosphate + L-lysine
phosphate + ?
-
-
-
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
carbamoyl phosphate + L-ornithine
phosphate + citrulline
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
carbamoyl phosphate + lysine
phosphate + homocitrulline
phosphate + L-citrulline
carbamoyl phosphate + L-ornithine
-
-
-
-
r
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
additional information
?
-
3'-hydroxymethylcephem + carbamoyl phosphate
cephamycin C + phosphate
-
-
-
?
3'-hydroxymethylcephem + carbamoyl phosphate
cephamycin C + phosphate
-
-
-
?
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
-
66fold higher activity with canaline than with ornithine
-
?
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
-
isoform 2 shows 13times higher canaline-dependent transcarbamoylase activity than ornithine-dependent transcarbamoylase activity
-
-
?
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
-
66fold higher activity with canaline than with ornithine, enzyme may play a role in canavanine synthesis
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
-
-
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
the enzyme produces Cit-Ala-hArg from tripeptide Orn-Ala-hArg and carbamyl phosphate as substrates
-
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
-
-
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
the enzyme produces Cit-Ala-hArg from tripeptide Orn-Ala-hArg and carbamyl phosphate as substrates
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
catalyzes the sixth step in arginine biosynthesis
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
catalyzes the sixth step in arginine biosynthesis
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
Arundinaria sp.
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
Arundinaria sp.
-
cytoplasmic form has predominantly catabolic function, mitochondrial form has anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
highly specific for L-ornithine at pH 8.0
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
isoform 1 shows 14times higher ornithine-dependent transcarbamoylase activity than canaline-dependent transcarbamoylase activity
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme seems to be involved in a bicarbonate-fixing pathway
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
highly specific for L-ornithine at pH 8.0
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme belongs to the arginine biosynthesis pathway
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
catabolic ornithine carbamoyltransferase, catalyzes the reverse reaction, i.e. the cleavage of citrulline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
ornithine transcarbamylase deficiency is the most common inherited disorder of the urea cycle and is transmitted as an X-linked trait, defects in the OTC gene, especially at clusters of the substrate binding sites, cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
the carbamoyl phosphate binding site contains the highly conserved motif Ser90-Thr91-Arg92-Thr93-Arg94, the ornithine binding site contains the His302-Cys303-Leu304-Pro305 motif
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme also catalyzes the reactions of EC 2.1.3.6, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase converting agmatine and ornithine into putrescine and citrulline
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme is involved in the biosynthesis of arginine in many organisms and participates in the urea cycle of mammals
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?, r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
very low activity with canaline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
catabolic ornithine carbamoyltransferase, catalyzes the reverse reaction, i.e. the cleavage of citrulline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
first step in arginine biosynthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
shark
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
catalyzes the last step of mitochondrial citrulline synthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme catalyzes the synthesis of delta-acetyl ornithine at 0.3-0.5% the rate of citrulline synthesis at pH 8.5 when acetyl phosphate replaces carbamoyl phosphate
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme catalyzes the synthesis of delta-acetyl ornithine at 0.3-0.5% the rate of citrulline synthesis at pH 8.5 when acetyl phosphate replaces carbamoyl phosphate
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + lysine
phosphate + homocitrulline
-
at alkaline pH
-
?
carbamoyl phosphate + lysine
phosphate + homocitrulline
-
at alkaline pH
-
?
carbamoyl phosphate + lysine
phosphate + homocitrulline
-
4.3% of the rate with ornithine
-
?
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
-
-
-
-
?
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
-
catabolic carbamoyltransferase
-
-
?
additional information
?
-
in addition to using putrescine, see EC 2.1.3.6, the enzyme can utilize L-ornithine as a poor substrate. Differences between the respective 230 and SMG loops of putrescine transcarbamoylase PTC and OTC appear to account for the differential preference of these enzymes for putrescine and ornithine, active center and the discrimination mechanism between putrescine and ornithine, overview
-
-
?
additional information
?
-
OTC-t1 and OTC-t2 transcripts display heterogeneity at the cleavage sites in a tissue-dependent manner
-
-
?
additional information
?
-
-
OTC-t1 and OTC-t2 transcripts display heterogeneity at the cleavage sites in a tissue-dependent manner
-
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
?
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
?
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
?
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
?
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
?
additional information
?
-
both substrates are unable to bind in a proper orientation in the active site pocket and this can be due to the differently oriented side chains. This suggests that the active site geometry should also undergo fine tuning besides the large structural changes as the enzyme switches from completely open to a substrate bound closed state
-
-
?
additional information
?
-
-
both substrates are unable to bind in a proper orientation in the active site pocket and this can be due to the differently oriented side chains. This suggests that the active site geometry should also undergo fine tuning besides the large structural changes as the enzyme switches from completely open to a substrate bound closed state
-
-
?
additional information
?
-
both substrates are unable to bind in a proper orientation in the active site pocket and this can be due to the differently oriented side chains. This suggests that the active site geometry should also undergo fine tuning besides the large structural changes as the enzyme switches from completely open to a substrate bound closed state
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
-
66fold higher activity with canaline than with ornithine, enzyme may play a role in canavanine synthesis
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
carbamoyl phosphate + L-ornithine
phosphate + citrulline
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
additional information
?
-
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
the enzyme produces Cit-Ala-hArg from tripeptide Orn-Ala-hArg and carbamyl phosphate as substrates
-
-
?
carbamoyl phosphate + L-Orn-Ala-hArg
phosphate + L-Cit-Ala-hArg
the enzyme produces Cit-Ala-hArg from tripeptide Orn-Ala-hArg and carbamyl phosphate as substrates
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
-
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
catalyzes the sixth step in arginine biosynthesis
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
catalyzes the sixth step in arginine biosynthesis
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
Arundinaria sp.
-
cytoplasmic form has predominantly catabolic function, mitochondrial form has anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme seems to be involved in a bicarbonate-fixing pathway
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme belongs to the arginine biosynthesis pathway
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
ornithine transcarbamylase deficiency is the most common inherited disorder of the urea cycle and is transmitted as an X-linked trait, defects in the OTC gene, especially at clusters of the substrate binding sites, cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
enzyme is involved in the biosynthesis of arginine in many organisms and participates in the urea cycle of mammals
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
anabolic function
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
first step in arginine biosynthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
catalyzes the last step of mitochondrial citrulline synthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
-
-
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
?
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
?
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
?
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
?
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
?
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2,4,6-Trinitrobenzenesulfonate
5,5'-dithiobis(2-nitrobenzoate)
5-hydroxy-2-aminovaleric acid
-
competitive vs. ornithine, uncompetitive vs. carbamoylphosphate
Acetylimidazole
-
50 mM, 95% inhibition at 25°C in 100 mM imidazole-HCl, pH 7.5
agmatine
-
13 mM, 50% inhibition
arginase
-
500 units, 14% remaining activity
-
arsenate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
Cd2+
-
1 mM, 99% inhibition
Chlorosis-inducing toxin of Pseudomonas phaseolicola
-
no more than 85% inhibition
-
citrulline
-
competitive to carbamoyl phosphate
Cu2+
-
1 mM, 75% inhibition
delta-N-(phosphonacetyl)-L-ornithine
delta-N-(phosphonoacetyl)-L-ornithine
bisubstrate analogue inhibitor
Delta-N-Phosphonoacetyl-L-ornithine
dithiodiglycol
-
100 mM, inactivation at pH 9,0
DL-2-Amino-5-hydroxypentanoic acid
L-2,4-diaminobutyric acid
L-2-Amino-4-pentenoic acid
-
-
L-cysteine
-
10 mM, 90% inhibition, noncompetitive vs. ornithine
MgCl2
-
10 mM, 14% inhibition
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
N5-[amino(sulfoamino)phosphoryl]-L-ornithyl-L-alanyl-N6-carbamimidoyl-L-lysine
-
inhibition of isoform 1 only
NaCl
-
50 mM, 25% inhibition
p-chloromercuribenzoate
-
-
Phenylglyoxal
-
complete inactivation after 1 h incubation
S-carbamoyl cysteine
-
10 mM, 90% inhibition
Tris
-
50 mM, more than 80% inhibition
1,4-diaminobutane
-
100 mM, 50% inhibition
1,4-diaminobutane
-
10 mM; 10 mM, 45% inhibition
2,4,6-Trinitrobenzenesulfonate
-
-
2,4,6-Trinitrobenzenesulfonate
-
10 mM, almost complete inactivation
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
complete inactivation at alkaline pH
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
complete inactivation at alkaline pH
ADP
5 mM, 90% inhibition
AMP
5 mM, 90% inhibition
arginine
-
L-isomer, 8 mM, 50% inhibition
arginine
-
several arginine analogs have no effect
arginine
-
5 mM, 42% inhibition
ATP
5 mM, 90% inhibition
Carbamoyl phosphate
-
-
CTP
5 mM, 90% inhibition
cystamine
-
complete inactivation, activity is completely recovered by incubation with 20 mM dithiothreitol
cystamine
-
complete inactivation, activity is completely recovered by incubation with 20 mM dithiothreitol
delta-N-(phosphonacetyl)-L-ornithine
-
-
delta-N-(phosphonacetyl)-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
competitive vs. carbamoylphosphate; transition state analogue
Delta-N-Phosphonoacetyl-L-ornithine
-
weak
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
0.001 mM, 86% inhibition, 0.0025 mM, 95% inhibition
Delta-N-Phosphonoacetyl-L-ornithine
-
transition state analogue
Delta-N-Phosphonoacetyl-L-ornithine
-
synthesis and properties
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
-
DL-2-Amino-5-hydroxypentanoic acid
-
-
DL-2-Amino-5-hydroxypentanoic acid
-
-
GTP
5 mM, 90% inhibition
iodoacetate
-
-
L-2,4-diaminobutyric acid
-
-
L-2,4-diaminobutyric acid
-
-
L-2,4-diaminobutyric acid
-
-
L-2,4-diaminobutyric acid
-
-
L-2-aminobutyrate
-
L-isomer
L-2-aminobutyrate
-
L-isomer
L-2-aminobutyrate
-
L-isomer
L-2-aminobutyrate
-
5-20 mM; L-isomer
L-alanine
-
-
L-isoleucine
-
-
L-leucine
-
-
L-lysine
-
weak
L-norleucine
-
-
L-norvaline
-
-
L-norvaline
-
2 mM, 50% inhibition
L-norvaline
-
competitive vs. ornithine, uncompetitive vs. carbamoylphosphate
L-norvaline
-
competitive vs. ornithine
L-ornithine
-
-
L-valine
-
-
methionine
-
L-isomer
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
trivial name phaseolotoxin, 0.1 mM, 93% inhibition
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
inhibition of isoform 1 only
ornithine
-
-
ornithine
-
at high concentrations
ornithine
-
at high concentrations
ornithine
-
at high concentrations; noncompetitive substrate inhibition vs. carbamoylphosphate
ornithine
-
recombinant wild-type enzyme
ornithine
-
at high concentrations
ornithine
-
competitive vs. carbamoylphosphate in the presence of phosphate
p-hydroxymercuribenzoate
-
inhibition is completely reversed by 2-mercaptoethanol
p-hydroxymercuribenzoate
-
inhibition is completely reversed by 2-mercaptoethanol
phosphate
-
-
phosphate
-
competitive vs. carbamoylphosphate
phosphate
-
competitive vs. carbamoylphosphate, uncompetitive vs. ornithine
phosphate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
phosphate
slight inhibition
phosphate
-
competitive vs. carbamoylphosphate
spermidine
-
10 mM, 93% inhibition, 3.7 mM, 50% inhibition
spermidine
-
E105G mutant enzyme, competitive vs. carbamoylphosphate
spermidine
-
10 mM, more than 98% inhibition of arsenolytic cleavage activity
UTP
5 mM, 90% inhibition
Zn2+
-
1 mM, 44% inhibition
additional information
-
effects of chemical modifications of specific residues on ligand binding and enzymatic activity
-
additional information
-
not inhibited by 10 mM 2-oxoglutarate, proline, glutamate, aspartate, acetylglutamate, pyruvate, oxaloacetate, glycine, acetylornithine, ATP, GTP, CTP, L-asparagine, arginine and glutamine
-
additional information
-
not inhibited by 10 mM 2-oxoglutarate, proline, glutamate, aspartate, acetylglutamate, pyruvate, oxaloacetate, glycine, acetylornithine, ATP, GTP, CTP, L-asparagine, arginine and glutamine
-
additional information
-
not inhibited by lysine and alpha-methyl-L-ornithine
-
additional information
-
not inhibited by 10 mM 2-oxoglutarate, proline, glutamate, aspartate, acetylglutamate, pyruvate, oxaloacetate, glycine, acetylornithine, ATP, GTP, CTP, L-asparagine, arginine and glutamine
-
additional information
-
effects of chemical modifications of specific residues on ligand binding and enzymatic activity
-
additional information
Ndelta(N'-sulfo-diaminophosphinyl)-ornithyl-alanyl-homoarginine and Ndelta (N'-sulfo-diaminophosphinyl)-ornithine are irreversible inhibitor of ornithine transcarbamylase attributed to the chemical structure similarity with tetrahedral intermediates in OTCase mechanism. But the enzyme from Pseudomona syringae pv. phaseolicola shows resistance against the phytotoxic compounds.Inhibition of OTCase blocks the biosynthesis of arginine in vivo and leads to a reduction of protein synthesis
-
additional information
-
isoform 2 is not inhibited by phaseolotoxin and ornithine-delta-P(O)(NH2)-NH-SO3H
-
additional information
-
not inhibited by arginine
-
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0.0008 - 1.4
Carbamoyl phosphate
0.033 - 0.25
Carbamoylphosphate
43.5
Diaminobutane
-
pH 8.5, 37°C
10.4
L-citrulline
-
pH 8.0, 37°C
25
L-lysine
-
pH 8.5, 37°C
2.3
phosphate
-
pH 8.0, 37°C
additional information
additional information
-
enzyme folding/unfolding kinetics and thermodynamics, overview
-
0.0008
Carbamoyl phosphate
-
liver enzyme, presence of putrescine, pH 7.0
0.00176
Carbamoyl phosphate
-
liver enzyme, pH 7.0
0.008
Carbamoyl phosphate
pH 8.0, 37°C
0.06
Carbamoyl phosphate
-
Q106E
0.09
Carbamoyl phosphate
-
pH 8.5, 37°C
0.13
Carbamoyl phosphate
-
pH 8.0, 37°C
0.13
Carbamoyl phosphate
-
wild-type, pH 7.7, 37°C
0.15
Carbamoyl phosphate
-
mutant K88R, pH 7.7, 37°C
0.15
Carbamoyl phosphate
mutant enzyme D231A, at pH 8.5 and 20°C
0.22
Carbamoyl phosphate
mutant enzyme E299D, at pH 8.5 and 20°C
0.26
Carbamoyl phosphate
mutant enzyme C273A, at pH 8.5 and 20°C
0.27
Carbamoyl phosphate
wild type enzyme, at pH 8.5 and 20°C
0.28
Carbamoyl phosphate
mutant enzyme R57A, at pH 8.5 and 20°C
0.3
Carbamoyl phosphate
mutant enzyme S61A, at pH 8.5 and 20°C
0.3
Carbamoyl phosphate
mutant enzyme Y160S, at pH 8.5 and 20°C
0.32
Carbamoyl phosphate
mutant enzyme Y229S, at pH 8.5 and 20°C
0.33
Carbamoyl phosphate
mutant enzyme Y229F, at pH 8.5 and 20°C
0.34
Carbamoyl phosphate
mutant enzyme E299Q, at pH 8.5 and 20°C
0.36
Carbamoyl phosphate
-
wild type
0.4
Carbamoyl phosphate
mutant enzyme Q104L, at pH 8.5 and 20°C
0.5
Carbamoyl phosphate
mutant enzyme H272N, at pH 8.5 and 20°C
0.53
Carbamoyl phosphate
mutant enzyme Y160F, at pH 8.5 and 20°C
0.625
Carbamoyl phosphate
-
pH 8.5, 10 mM fixed substrate
0.9
Carbamoyl phosphate
-
pH 9.0, 30°C
0.93
Carbamoyl phosphate
mutant enzyme H272L, at pH 8.5 and 20°C
1
Carbamoyl phosphate
-
pH 9.0, 20°C
1.1
Carbamoyl phosphate
-
pH 9.0, 5°C
1.24
Carbamoyl phosphate
-
mutant K88Q, pH 7.7, 37°C
1.4
Carbamoyl phosphate
mutant enzyme D140N, at pH 8.5 and 20°C
0.033
Carbamoylphosphate
-
37°C, pH 8.6
0.087
Carbamoylphosphate
-
37°C, pH 8.2
0.25
Carbamoylphosphate
-
37°C, pH 9.0
0.001
L-ornithine
-
liver enzyme, presence of putrescine, pH 7.0
0.00232
L-ornithine
-
liver enzyme, pH 7.0
0.0285
L-ornithine
pH 8.0, 37°C
0.05
L-ornithine
-
mutant K268A, pH 8.0, 30°C
0.11
L-ornithine
-
pH 8.0, 37°C
0.25
L-ornithine
-
37°C, pH 8.6
0.33
L-ornithine
-
37°C, pH 8.2
0.33
L-ornithine
mutant enzyme E299Q, at pH 8.5 and 20°C
0.36
L-ornithine
-
wild-type, pH 7.7, 37°C
0.4
L-ornithine
mutant enzyme H272N, at pH 8.5 and 20°C
0.42
L-ornithine
-
mutant K88R, pH 7.7, 37°C
0.44
L-ornithine
mutant enzyme R57A, at pH 8.5 and 20°C
0.45
L-ornithine
-
37°C, pH 9.0
0.45
L-ornithine
mutant enzyme Y229F, at pH 8.5 and 20°C
0.53
L-ornithine
mutant enzyme S61A, at pH 8.5 and 20°C
0.53
L-ornithine
wild type enzyme, at pH 8.5 and 20°C
0.55
L-ornithine
-
mutant K88Q, pH 7.7, 37°C
0.59
L-ornithine
mutant enzyme D231A, at pH 8.5 and 20°C
0.61
L-ornithine
mutant enzyme Y229S, at pH 8.5 and 20°C
0.68
L-ornithine
mutant enzyme H272L, at pH 8.5 and 20°C
0.73
L-ornithine
mutant enzyme C273A, at pH 8.5 and 20°C
0.81
L-ornithine
mutant enzyme Q104L, at pH 8.5 and 20°C
0.9
L-ornithine
mutant enzyme E299D, at pH 8.5 and 20°C
1
L-ornithine
-
mutant K260A, pH 8.0, 30°C
1
L-ornithine
mutant enzyme Y160F, at pH 8.5 and 20°C
1.1
L-ornithine
-
pH 8.5, 37°C
1.1
L-ornithine
-
mutant K265R, pH 8.0, 30°C
1.1
L-ornithine
-
mutant K268R, pH 8.0, 30°C
1.2
L-ornithine
-
mutant E256Q, pH 8.0, 30°C
1.2
L-ornithine
-
mutant K260R, pH 8.0, 30°C
1.2
L-ornithine
-
mutant K265A, pH 8.0, 30°C
1.3
L-ornithine
-
mutant Q294P, pH 8.0, 30°C
1.6
L-ornithine
-
wild-type, pH 8.0, 30°C
1.78
L-ornithine
-
pH 9.0, 5°C
2
L-ornithine
-
mutant L290Q, pH 8.0, 30°C
2
L-ornithine
-
mutant L290S, pH 8.0, 30°C
2.1
L-ornithine
-
mutant E123S, pH 8.0, 30°C
2.6
L-ornithine
-
mutant E123A, pH 8.0, 30°C
2.8
L-ornithine
-
mutant C191M/C194N/F197V, pH 8.0, 30°C
3.34
L-ornithine
-
pH 9.0, 10°C
3.4
L-ornithine
-
mutant T68G, pH 8.0, 30°C
5.67
L-ornithine
-
pH 9.0, 15°C
7.3
L-ornithine
mutant enzyme Y160S, at pH 8.5 and 20°C
8
L-ornithine
-
pH 9.0, 20°C
10
L-ornithine
-
mutant E256A, pH 8.0, 30°C
10
L-ornithine
-
mutant K289S, pH 8.0, 30°C
17
L-ornithine
mutant enzyme D140N, at pH 8.5 and 20°C
20
L-ornithine
-
mutant K263R, pH 8.0, 30°C
22.49
L-ornithine
-
pH 9.0, 25°C
30
L-ornithine
-
mutant K263A, pH 8.0, 30°C
32
L-ornithine
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C
34
L-ornithine
-
mutant N184Q, pH 8.0, 30°C
36.4
L-ornithine
recombinant wild-type enzyme, pH 8.5, 37°C
45
L-ornithine
-
pH 9.0, 30°C
49
L-ornithine
-
mutant D182N, pH 8.0, 30°C
350
L-ornithine
-
mutant N185Q, pH 8.0, 30°C
0.8
ornithine
-
wild type, pH 7.25
0.85
ornithine
-
pH 8.5, 10 mM fixed substrate
1.8
ornithine
-
mutant arcB6254, pH 7.25
1.85
ornithine
-
mutant arcB6240, pH 7.25
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0.00058
-
crude cell extract
0.0928
-
isoenzyme 2 with ornithine
0.255
-
pH 8.0, 55°C, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
0.43
-
pH 8.0, 55°C, activity in cell culture in growth medium with 0.5% peptone and 0.1% yeast extract
0.47
-
multifunctional enzyme
0.574
-
isoenzyme 1 with canaline
1.24
-
isoenzyme 2 with canaline
1.28
-
mutant T68G, pH 8.0, 30°C
12.33
-
mutant N184Q, pH 8.0, 30°C
12.66
-
mutant E256Q, pH 8.0, 30°C
12.67
-
pH 7.5, crude cell exstract
13.3
-
mutant L290Q, pH 8.0, 30°C
14.83
-
mutant K263R, pH 8.0, 30°C
15
-
mutant E256A, pH 8.0, 30°C
16.16
-
mutant D182N, pH 8.0, 30°C
16.83
-
mutant K265A, pH 8.0, 30°C
2.33
-
extracts prepared from Escherichia coli CM236 carrying pME178
2.83
-
mutant K289S, pH 8.0, 30°C
23.38
-
mutant E123S, pH 8.0, 30°C
23.63
-
mutant K265R, pH 8.0, 30°C
24
recombinant wild-type enzyme, substrate L-ornithine, pH 8.5, 37°C
25.16
-
mutant K260R, pH 8.0, 30°C
25.3
-
mutant E123A, pH 8.0, 30°C
25.73
-
mutant K268R, pH 8.0, 30°C
25.83
-
mutant K260A, pH 8.0, 30°C
26.12
-
wild-type, pH 8.0, 30°C
3.33
-
recombinant enzyme
3.59
-
anabolic reaction, pH 10.0, 37°C
4.16
-
mutant C191M/C194N/F197V, pH 8.0, 30°C
4.66
-
mutant L290S, pH 8.0, 30°C
40.2
-
recombinant enzyme
450
-
pH 7.5, purified enzyme
48.66
-
mutant Q294P, pH 8.0, 30°C
7.5
-
mutant K263A, pH 8.0, 30°C
8.31
-
isoenzyme 1 with ornithine
82
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, substrate L-ornithine, pH 8.5, 37°C
83.3
-
enzyme from a liver of a Reye's syndrome patient
86.5
-
enzyme from normal liver
0.12
-
catabolic reaction, pH 5.0-6.0, 37°C
0.12
-
pH 8.0, 55°C, activity in cell culture in growth medium with 0.2% yeast extract
25
-
mutant K268A, pH 8.0, 30°C
25
-
mutant N185Q, pH 8.0, 30°C
additional information
highest activity at 4 M KCl
additional information
-
highest activity at 4 M KCl
additional information
-
enzyme activity during mechanical jaundice in the rat model
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evolution
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
evolution
-
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
-
malfunction
-
absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
malfunction
-
inborn deficiency of OTC causes mainly urea cycle-related disorders and leads to hyperammonemic states that may become lethal. Some states of hepatotoxicity are associated woth hepatocyte disruption and release of OTC into the bloodstream
malfunction
-
absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
-
metabolism
-
the binding of carbamoyl phosphate to the enzymes aspartate and ornithine transcarbamoylase reduces the rate of thermal decomposition of carbamoyl phosphate by a factor of >5000. Both of these transcarbamoylases use an ordered-binding mechanism in which carbamoyl phosphate binds first, allowing the formation of an enzyme-carbamoyl phosphate complex. The critical step in the thermal decomposition of carbamoyl phosphate in aqueous solution, in the absence of enzyme, involves the breaking of the C-O bond facilitated by intramolecular proton transfer from the amine to the phosphate. The binding of carbamoyl phosphate to the active sites of the enzymes significantly inhibits this process by restricting the accessible conformations of the bound ligand to those disfavoring the reactive geometry
metabolism
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
metabolism
-
ArgF is involved in the biosynthesis of L-arginine, overview
metabolism
-
catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of arginine deiminase and agmatine deiminase pathways. However, the equilibrium of in vitro carbamoyltransfer reactions is overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase is probably the limiting step of the pathways. lmo0036 is induced at the transcriptional level when Listeria monocytogenes is subjected to low-pH stress. Its expression product in Escherichia coli exhibits higher catabolic carbamoyltransfer activities under acidic conditions
metabolism
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
metabolism
-
the enzyme is a mitochondria matrix urea cycle enzyme that is primarily expressed in hepatocyte
metabolism
carbamoyl-phosphate synthetase and ornithine carbamoyltransferase form an efficient channeling cluster for carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate. Therefore, by physically interacting with each other, carbamoyl-phosphate synthetase and ornithine carbamoyltransferase prevent the thermodenaturation of carbamoyl phosphate in the aqueous cytoplasmic environment
metabolism
-
the enzyme activity supports nitric oxide production in nitrergic neurons
metabolism
-
the enzyme is a mitochondria matrix urea cycle enzyme that is primarily expressed in hepatocyte
-
metabolism
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
metabolism
-
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
-
metabolism
-
catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of arginine deiminase and agmatine deiminase pathways. However, the equilibrium of in vitro carbamoyltransfer reactions is overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase is probably the limiting step of the pathways. lmo0036 is induced at the transcriptional level when Listeria monocytogenes is subjected to low-pH stress. Its expression product in Escherichia coli exhibits higher catabolic carbamoyltransfer activities under acidic conditions
-
physiological function
insertion mutant shows arginine auxotrophy and formes infection threads for symbiosis with Lotus japonicus, but the nodules formed have few infected cells filled with bacteroids
physiological function
arginine biosynthesis
physiological function
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
physiological function
OTC catalyzes the reversible transfer of the carbamoyl group from carbamoyl phosphate to the Nepsilon atom of L-ornithine to produce L-citrulline. There are two types of enzyme: anabolic, aOTC, and catabolic, cOTC. Anabolic OTCs catalyze the forward reaction and participate in the urea cycle and L-arginine biosynthesis
physiological function
-
OTC is involved in the metabolic transformation of arginine and proline and participates in the urea cycle. OTC is regulated by glucocorticoids and other transcriptional factors, such as C/EFP and HNF-4. OTC is released into the blood stream from liver in case of liver regeneration cell proliferation, extracellular might play a role as signaling molecule
physiological function
the OTC activity of the enzyme is involved in arginine biosynthesis
physiological function
-
physically interacting with each other, carbamate kinase and ornithine carbamoyltransferase prevent thermodenaturation of carbamoyl phosphate (a precursor of pyrimidines and arginine, which is an extremely labile and potentially toxic intermediate) in the aqueous cytoplasmic environment. The carbamoyl phosphate channelling complex involves carbamate kinase, ornithine carbamoyltransferase and aspartate carbamoyltransferase
physiological function
the enzyme ArgK in Pseudomona syringae pv. phaseolicola is resonsible for self-defense in the antimetabolic phytotoxin phaseolotoxin, a sulfodiaminophosphinyl tripeptide produced to inhibit plant host cell's ornithine transcarbamylase activity and induce arginine auxotrophic phenotype. Phaseolotoxin-resistant OTCase ArgK acts as a functional replacement of housekeeping OTCase ArgF, which is the acting target of phaseolotoxin, to confer phaseolotoxin producers with self-resistance. But neither transcriptional regulator nor thermal regulation related protein encoding gene is detected from PHT biosynthetic gene cluster
physiological function
the enzyme induces proinflammatory cytokine gene expression by activating NF-kappaB in macrophages of the bovine host. The enzyme plays a role in induction of upregulation of interferon-gamma and proinflammatory cytokines (interleukin-1beta, IL-6, and tumor necrosis factor-alpha) in Bos taurus Ana-1 macrophages
physiological function
-
the enzyme which is involved in bacterial adherence, may efficiently stimulate an immune response conferring protection against Streptococcus suis infections
physiological function
-
the enzyme ArgK in Pseudomona syringae pv. phaseolicola is resonsible for self-defense in the antimetabolic phytotoxin phaseolotoxin, a sulfodiaminophosphinyl tripeptide produced to inhibit plant host cell's ornithine transcarbamylase activity and induce arginine auxotrophic phenotype. Phaseolotoxin-resistant OTCase ArgK acts as a functional replacement of housekeeping OTCase ArgF, which is the acting target of phaseolotoxin, to confer phaseolotoxin producers with self-resistance. But neither transcriptional regulator nor thermal regulation related protein encoding gene is detected from PHT biosynthetic gene cluster
-
physiological function
-
OTC catalyzes the reversible transfer of the carbamoyl group from carbamoyl phosphate to the Nepsilon atom of L-ornithine to produce L-citrulline. There are two types of enzyme: anabolic, aOTC, and catabolic, cOTC. Anabolic OTCs catalyze the forward reaction and participate in the urea cycle and L-arginine biosynthesis
-
physiological function
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
-
physiological function
-
the enzyme which is involved in bacterial adherence, may efficiently stimulate an immune response conferring protection against Streptococcus suis infections
-
physiological function
-
physically interacting with each other, carbamate kinase and ornithine carbamoyltransferase prevent thermodenaturation of carbamoyl phosphate (a precursor of pyrimidines and arginine, which is an extremely labile and potentially toxic intermediate) in the aqueous cytoplasmic environment. The carbamoyl phosphate channelling complex involves carbamate kinase, ornithine carbamoyltransferase and aspartate carbamoyltransferase
-
additional information
sequence 230YGLY233 is the putrescine signature sequence
additional information
-
stochastic simulations of coarse-grained protein models used to investigate the propensity to form knots in early stages of protein folding, comparison of natively-knotted N-acetylornithine carbamoyltransferase, AOTCase, EC 2.1.3.9, and an unknotted ornithine carbamoyltransferase, OTCase, protein and amino acid interactions, mechanism, overview. The different entanglement of the two transcarbamylases follows from the tendency of the C-terminal to point away from (for OTCase) or approach and eventually thread (for AOTCase) other regions of partly-folded protein. The analysis of the OTCase/AOTCase pair clarifies that natively-knotted proteins can spontaneously knot during early folding stages and that non-native sequence-dependent interactions are important for promoting and disfavouring early knotting events. Knotting usually results from the threading of the C-terminal through loops present in the loose protein globule. Simulation of the early folding process of the two transcarbamylases, non-native interactions, kinetics, and modeling, overview
additional information
the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
additional information
-
the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
additional information
-
the enzyme is released in response to drugs
additional information
the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
additional information
-
the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
additional information
-
the enzyme is released in response to drugs
-
additional information
-
the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
-
additional information
-
the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
-
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unliganded aOTC, hanging drop vapor diffusion method, mixing of 500 nl 10 mg/ml protein solution with 500 nl well solution containing 25% PEG 3350, 0.2 M NaCl, 0.1 M HEPES, pH 8.0, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement and modeling
purified full-length enzyme or in complex with inhibitors N-(phosphonoacetyl)-putrescine or N-(phosphonoacetyl)-L-ornithine, and trunacted enzyme in complex with N-(phosphonoacetyl)-L-ornithine, hanging drop vapor diffusion technique, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5 containing 0.43 mM ligand with 0.001 ml of crystallization solution composed of 125 mM (NH4)2SO4, 17% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 21°C, X-ray diffraction structure determination and analysis at 2.5 A, 2.0 A, and 1.59 A resolution, respectively, modeling
ornithine carbamoyltransferase-Ndelta-(N'-sulfodiaminophosphinyl)-L-ornithine complex, hanging-drop vapour diffusion, equal volumes of protein are combined with a solution containing 17.8% polyethylene glycol 8000 and 2.2% polyethylene glycol 1000, pyramidal crystals after 1-2 weeks
one protein molecule per asymmetric unit, trimeric structure
-
complexed with the bisubstrate analog N-phosphoacetyl-L-ornithine
-
ornithine transcarbamoylase-carbamoylphosphate complex, X-ray structure at 2.4-2.6 A resolution
hanging drop vapor diffusion method
-
to 2.1 A resolution. enzyme forms a homohexamer with 32 point group symmetry. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution
hanging drop vapor diffusion method, crystal structures of Mtb OTC in orthorhombic and hexagonal form hexagonal form crystals complexed with carbamoyl phosphate and L-norvaline
crystal structure determination of the E105G mutant at 3.0 A resolution
-
T allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 100 mM glycylglycin, pH 9, 12% polyethylene glycol 6000 and 1 mM dithiothreitol, X-ray analysis, 4.5 A resolution, R allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 1.9 M ammonium sulfate, 50 mM HEPES, pH 7.2, 1 mM DTT, 1 mM EDTA, 3% polyethylene glycol 400 and 10 mM spermidine
-
dodecamer, four catalytic trimers disposed in a tetrahedral manner
-
hanging-drop vapor diffusion, 1/1 mixture of 12 mg/ml enzyme solution and a reservoir solution containing 1 M NaCl, 100 mM acetate buffer, pH 4.0, crystals are obtained after 7-10 days, X-ray structure at 2.7 A resolution
-
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of well solution containing 10% PEG 4000, 0.1 M NaCl, 0.1 M HEPES-Na, pH 7.5, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling
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H121R
-
isoform 2, 80% increase in ornithine dependent activity, 64% decrease in canaline-dependent activity
R54G
site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity
Y230V/G231S/L232M/Y233G
engineering of the 230-loop of the enzyme, by replacing the sequence 230YGLY233 of the putrescine signature by its OTC counterpart VSMG, favors the use of ornithine and impairs that of putrescine
C273A
the mutant shows 2.8 and 3.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D140N
the mutant shows 5.4 and 28fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D231A
the mutant shows 450 and 580fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299D
the mutant shows 2.5 and 4.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299Q
the mutant shows 110 and 51fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272L
the mutant shows 310 and 120fold and decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272N
the mutant shows 4.2 and 3.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q104L
the mutant shows 5.9 and 10fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q106E
-
mutant to study the carbamoyl phosphate cooperativity on the anabolic OTCase
R57A
the mutant shows 57 and 44fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
S61A
the mutant shows 6.1 and 1.8fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160F
the mutant shows 6.7 and 8.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160S
the mutant shows 1.5 and 14fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229F
the mutant shows 3.5 and 2.7fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229S
the mutant shows 1.7 and 1.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
K88Q
-
less than 1% of wild-type activity
K88R
-
mutant retains substantial enzymatic activity
R277W
-
shows no substrate inhibition by ornithine, 70fold lower affinity for L-ornithine
E106A
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mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106G
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mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106A
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mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
-
E106G
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mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
-
A240D
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10fold increase of Km at 55°C
E277G
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14fold increase of Km at 55°C
Y227D
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slight increase of Km at 55°C
D182N
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greatly reduced affinity for L-ornithine, no interaction with arginase
E123A
-
little change in activity, or in sensitivity to arginase
E123S
-
little change in activity, or in sensitivity to arginase
E256A
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
E256Q
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
G181R
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no residual activity
K260A
-
important in mediating sensitivity to L-ornithine and arginase
K260R
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important in mediating sensitivity to L-ornithine and arginase
K263R
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important in mediating sensitivity to L-ornithine and arginase
K265A
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important in mediating sensitivity to L-ornithine and arginase
K265R
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important in mediating sensitivity to L-ornithine and arginase
K268A
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important in mediating sensitivity to L-ornithine and arginase
K268R
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important in mediating sensitivity to L-ornithine and arginase
K289S
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
L290Q
-
reduced activity, little change in sensitivity to arginase
L290S
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reduced activity, little change in sensitivity to arginase
N184Q
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
N185Q
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
Q294P
-
little change in activity, or in sensitivity to arginase
T68G
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greatly reduced activity, no change in sensitivity to arginase
L118M
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isoform 2, 515% increase in ornithine dependent activity, 54% decrease in canaline-dependent activity
L118M
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isoform 2, 617% increase in ornithine dependent activity, 55% decrease in canaline-dependent activity
E105G
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no cooperativity towards carbamoyl phosphate, follows Michaelis-Menten kinetics
E105G
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mutant blocked in the active R (relaxed) state
additional information
-
construction of the putrescine-producing strain PUT1 by deletion of argF, the gene for ornithine transcarbamoylase, and argR, encoding the L-arginine repressor, combined with heterologous expression of the Escherichia coli gene for L-ornithine decarboxylase SpeC. The strain requires supplementation of L-arginine and shows growth-decoupled putrescine production. By fine-tuning argF expression through modifications of the promoter, the translational start codon and/or the ribosome binding site, high productivity and titer can be obtained, optimization of putrescine production by mutant strains, overview
additional information
confirmation of decreased stability of the trimer of the enzyme lacking the C-terminal helix by deleting this helix
additional information
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screening and analysis of naturally occuring mutations and polymorphisms in the OTC gene, defects in the OTC gene cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death, phenotypes of mutated individuals, overview
additional information
computer model of molecular dynamic
additional information
-
construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
additional information
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construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
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additional information
generation of in-frame deletion mutants of ArgK
additional information
-
generation of in-frame deletion mutants of ArgK
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additional information
-
null mutant of argK encoding phaseolotoxin resistant isozyme, enzyme expression is independent of temperature and regulated directly by a compound resembling the inorganic moiety of phaseolotoxin
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60-65°C for 5 min, ammonium sulfate, DEAE-cellulose, Bio-Gel P-300
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affinity chromatography on delta-N-(phosphonacetyl)-L-ornithine, Sephacryl S-200
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ammonium sulfate, 70°C for 25 min, gel filtration, ion-exchange chromatography
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ammonium sulfate, DEAE-cellulose, aminohexyl-agarose
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ammonium sulfate, DEAE-cellulose, isoforms 1 and 2
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ammonium sulfate, DEAE-Sephadex, Sephadex G-200
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ammonium sulfate, DEAE-Sepharose, ornithine[AcPO(OH)2]-Sepharose
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ammonium sulfate, heat treatment, celite, DEAE-Sephadex A-50, Sephacryl S-200, partial purification
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ammonium sulfate, heat, activated charcoal, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
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ammonium sulfate, Sephacryl S-200, delta-N-phosphonoacetyl-L-ornithine affinity chromatography
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ammonium sulfate, streptomycin, DEAE-cellulose, heating, DEAE-Sephadex
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DEAE-cellulose, isoelectric focusing
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DEAE-Sephacel, hydroxylapatite, preparative PAGE, isoenzyme 1
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DEAE-Sephadex, hydoxyapatite C, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
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delta-N-(phosphonoacetyl)-L-ornithine-Sepharose 6B affinity chromatography
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enzyme from normal liver and liver of a Reye's syndrome patient, DEAE-cellulose, hydroxylapatite, Sephadex G-200
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gel filtration, ammonium sulfate-mediated hydrophobic chromatography
gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
heat treatment, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
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heat, ammonium sulfate, DEAE-cellulose, hydroxylapatite, DEAE-Sephacel, Bio-Gel A 1.5
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heat, ammonium sulfate, DEAE-Sephadex, Sephadex G-200, aminohexyl-Sepharose
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high-performance hydrophobic interaction chromatography
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HisTrap column chromatography and Superdex 200 gel filtration
N-delta-(phosphonoacetyl)ornithine affinity chromatography, Sephadex G-100
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native enzyme by affinity chromatography using delta-N-(phosphonacetyl)-L-ornithine
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native enzyme from liver mitochondria by anion exchange chromatography, ultrafiltration, and gel filtration, to about 50% purity
-
Ni-NTA column chromatography
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plasmid-containing enzyme-overproducing strain
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protamine sulfate, ammonium sulfate, diethylaminoethyl-cellulose, Sephadex G-150, hydroxylapatite
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putrescine synthase has inherent activities of agmatine iminohydrolase, putrescine carbamoyltransferase, ornithine carbamoyltransferase and carbamate kinase, ammonium sulfate, putrescine-Sepharose affinity column
-
recombinant enzyme, Mono Q, arginine-Sepharose column
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recombinant enzyme, thermodenaturation at 85°C, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
recombinant His-tagged enzyme
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
recombinant protein using His-tag
-
recombinant wild-type and R277W mutant enzyme, ammonium sulfate, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
single step procedure using delta-N-(phosphonoacetyl)-L-ornithine-Sepharose 6B affinity chromatography
-
-
-
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analysis
-
after administration of carbon tetrachloride, allyl alcohol, D-galactosamine, lipopolysaccharide, and concanavalin A, the significant increase in the serum levels of the markers is faster in type-I arginase and ornithine carbamoyltransferase than aspartate aminotransferase and alanine aminotransferase. The extent of the increase at the peak is always higher in type-I arginase and ornithine carbamoyltransferase than in spartate aminotransferase and alanine aminotransferase
biotechnology
-
HepG2 is an immortalized human hepatoma cell line that has been used for research into bioartificial liver systems. However, a low level of ammonia detoxification is its biggest drawback. Stable overexpression of arginase I and ornithine transcarbamylase in HepG2 cells improves its ammonia detoxification
diagnostics
-
the enzyme alone or in combination with other markers is a useful indicator for Kupffer cell activation as well as for mitochondrial damage in hepatic cells
diagnostics
-
ornithine carbamoyltransferase is one promising blood-based biomarker candidate for liver injury examination
diagnostics
-
the enzyme can be used as biomarker for early stage of hepatic injury induced by CCl4, diagnostics values are best in combination with total bile acid and phosphorylase measurements
diagnostics
-
ornithine carbamoyltransferase is one promising blood-based biomarker candidate for liver injury examination
-
diagnostics
-
the enzyme can be used as biomarker for early stage of hepatic injury induced by CCl4, diagnostics values are best in combination with total bile acid and phosphorylase measurements
-
medicine
-
after administration of carbon tetrachloride, allyl alcohol, D-galactosamine, lipopolysaccharide, and concanavalin A, the significant increase in the serum levels of the markers is faster in type-I arginase and ornithine carbamoyltransferase than aspartate aminotransferase and alanine aminotransferase. The extent of the increase at the peak is always higher in type-I arginase and ornithine carbamoyltransferase than in spartate aminotransferase and alanine aminotransferase
medicine
-
in patients with Alzheimer's disease, ornithine carbamoyltransferase is expressed in brain, but not in controls. Ornithine carbamoyltransferase expression is strictly restricted to vascular endothelial cells. Ornithine carbamoyltransferase activity is 880% increased in the cerebrospinal fluid of probable Alzheimer's disease cases compared with controls. Rare haplotypes may be associated with the risk of Alzheimer's disease through a possible modulation of the methylation of the ornithine carbamoyltransferase promoter
medicine
-
in patients with non-alcoholic steatohepatitis, the serum levels of ornithine carbamoyltransferase and the ratios of ornithine carbamoyltransferase:alanine amino transferase and ornithine carbamoyltransferase:aspartate amino transferase are increased in parallel with the progression of on-alcoholic steatohepatitis. Especially, ornithine carbamoyltransferase and both ratios are markedly increased in hepatocellular carcinoma. As for the relationship between fibrosis grade and ornithine carbamoyxltransferase, the serum ornthine carbamoyltransferase levels and theratio of ornithine carbamoyltransferase:alanine amino transferase levels are increased in parallel with liver fibrosis. In non-alcoholic steatohepatitis patients with alanine amino transferase within normal range, about 30% show elevation of ornithine carbamoyltransferase
medicine
-
ornithine carbamoyltransferase is acetylated at lysine resiudes, including K88, which is also mutated in ornithine carbamoyltransferase-deficient patients. K88 acetylation decreases the affinity for carbamoyl phosphate, and the maximum velocity, whereas the Km for ornithine is not affected
medicine
ornithine carbamyltransferase is present in urine of patients with pulmonary tuberculosis. Recombinant ornithine carboamyltransferase produced in Escherichia coli is recognized by immunoglobulin G antibodies from patients with active tuberculosis but not by IgG from uninfected healthy subjects. Protein is strongly recognized by peripheral blood mononuclear cells from both healthy tuberculin purified protein derivative-positive individuals and patients with pulmonary tuberculosis
medicine
-
the serum activities of ornithine carbamoyltransferase and glutamate dehydrogenase increase significantly by chronic ethanol feeding while other markers do not. Although the hepatic content of ornithine carbamoyltransferase and glutamate dehydrogenase also increase, the serum activities do not correlate with the hepatic activities and the extent of increase in the liver is much less than in serum
medicine
-
use of multiplex ligation-dependent probe amplification methodology to three ornithine transcarbamylase deficiency patients, two females and one male, reveals copy number alterations of ornithine transcarbamylase exons in all of them. The two females are heterozygous for deletions of either exon 2 or exons 6-9, and the male is confirmed to lack all exons. Females' characterization of the deletion breakpoints reveal mutations corresponding to exon 2 and exon 6-9 deletions, respectively. Exon 2 deletion probably results from replication slippage facilitated by a secondary structure formed by two inverted Alu repeats, whereas an Alu-Alu homologous recombination is probably responsible for the exon 6_9 deletion
medicine
-
enzyme downregulation is associated with poor prognosis in hepatocellular carcinoma
medicine
-
measurement of serum enzyme concentration is a useful marker of disease severity, and thus can be a useful marker for a high risk of hepatocellular carcinoma occurrence
medicine
-
ornithine carbamyltransferase is present in urine of patients with pulmonary tuberculosis. Recombinant ornithine carboamyltransferase produced in Escherichia coli is recognized by immunoglobulin G antibodies from patients with active tuberculosis but not by IgG from uninfected healthy subjects. Protein is strongly recognized by peripheral blood mononuclear cells from both healthy tuberculin purified protein derivative-positive individuals and patients with pulmonary tuberculosis
-