Information on EC 2.1.3.11 - N-succinylornithine carbamoyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.3.11
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RECOMMENDED NAME
GeneOntology No.
N-succinylornithine carbamoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase
This enzyme is specific for N-succinyl-L-ornithine and cannot use either L-ornithine (see EC 2.1.3.3, ornithine carbamoyltransferase) or N-acetyl-L-ornithine (see EC 2.1.3.9, N-acetylornithine carbamoyltransferase) as substrate. However, a single amino-acid substitution (Pro90 -> Glu90) is sufficient to switch the enzyme to one that uses N-acetyl-L-ornithine as substrate. It is essential for de novo arginine biosynthesis in the obligate anaerobe Bacteroides fragilis, suggesting that this organism uses an alternative pathway for synthesizing arginine.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-69-8
cf. EC 2.1.3.3
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-ornithine + carbamoyl phosphate
N-acetyl-L-citrulline + phosphate
show the reaction diagram
N-succinyl-L-ornithine + carbamoyl phosphate
N-succinyl-L-citrulline + phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0119
N-acetyl-L-ornithine
mutant P90E/T242L, pH 8.3, 25C
0.0016 - 0.238
N-succinyl-L-ornithine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
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mutant E92P of N-acetyl-L-ornithine carbamoyltransferase, pH 8.3, 25C
29.8
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mutant E92A of N-acetyl-L-ornithine carbamoyltransferase, pH 8.3, 25C
40.5
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mutant E92V of N-acetyl-L-ornithine carbamoyltransferase, pH 8.3, 25C
66.9
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mutant E92S, pH 8.3, 25C
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with carbamyl phosphate and N-succinyl-L-norvaline, as well as sulfate and N-succinyl-L-norvaline, diffraction to 2.9 and 2.8 A resolution, respectively
mutant P90E, in complex with carbamoyl phosphate and N-acetyl-L-norvaline or N-succinyl-L-norvaline
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mutants E92P, E92S, E92V, E92A, in complex with carbamoyl phosphate and N-acetyl-L-norvaline or N-succinyl-L-norvaline
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P90E
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conversion of N-succinly-L-ornithine carbamoyltransferase to N-acetyl-L-ornithine carbamoyltransferase
P90E/T242L
contrary to wild-type, mutant accepts N-acetyl-L-ornithine as a substrate. Decrease in Km value for N-succinyl-L-ornithine
T242L
slight decrease in Km value
E92A
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site-directed mutagenesi of N-acetyl-L-ornithine carbamoyltransferase, conversion to N-succinly-L-ornithine carbamoyltransferase
E92P
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site-directed mutagenesi of N-acetyl-L-ornithine carbamoyltransferase, conversion to N-succinly-L-ornithine carbamoyltransferase
E92S
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site-directed mutagenesi of N-acetyl-L-ornithine carbamoyltransferase, conversion to N-succinly-L-ornithine carbamoyltransferase
E92V
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site-directed mutagenesi of N-acetyl-L-ornithine carbamoyltransferase, conversion to N-succinly-L-ornithine carbamoyltransferase