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Information on EC 3.5.1.20 - citrullinase
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3.5.1.20 citrullinaseSpecify your search results
Word Map
- 3.5.1.20
- tularensis
- francisella
- polyamine
-
protozoan
- novicida
-
subsp
- l-arginine
-
ciliated
- putrescine
-
ornithine-oxo-acid
- thermophila
-
avirulent
-
pasteurella
- l-ornithine
- tetrahymena
- tularemia
-
biovars
- holarctica
-
subspecies
-
octase
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
citrulline hydrolase, citrulline ureidase, CTU, L-citrulline N5-carbamoyldehydrolase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
citrulline hydrolase
citrulline ureidase
CTU
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-citrulline + H2O = L-ornithine + CO2 + NH3
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-citrulline N5-carbamoyldihydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
59088-17-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-citrulline + H2O
L-ornithine + CO2 + NH3
-
-
-
?
L-citrulline + H2O
?
Euphorbia sp.
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
enzyme is specific for citrulline, no hydrolysis of arginine, argininosuccinate, or other guanidino compounds
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
Phytomonas davidi
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-citrulline + H2O
L-ornithine + CO2 + NH3
-
-
-
?
L-citrulline + H2O
?
Euphorbia sp.
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
enzyme is specific for citrulline, no hydrolysis of arginine, argininosuccinate, or other guanidino compounds
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
Phytomonas davidi
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
L-citrulline + H2O
?
-
first intermediate in urea cycle, involved in arginine biosynthesis
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
-
stable up to 40°C for 10 min, retains 87% activity after treatment at 50°C, activity completely lost at 60°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Phytomonas davidi
trypanosomatide, parasite in euphorbs and asclepiads and other plants
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
citrulline ureidase is highly expressed in Francisella tularensis subsp. tularensis Schu S4 when compared to Francisella novicida U112, suggesting that it may contribute to the relative high virulence of Francisella tularensis subsp. tularensis Schu S4
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q5NHL7_FRATT
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
286
0
32430
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
generation of a nonpolar deletion DELTActu mutant. Deletion of the ctu gene results in loss of CTU activity, which is restored by transcomplementing the ctu gene. Loss of CTU does not affect acellular growth, but attenuates intramacrophage survival. Mice infected intranasally with the DELTActu mutant show significantly reduced bacterial burden in the lungs, liver, and spleen compared to wild-type Schu S4-infected mice.
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
-
stable up to 40°C for 10 min, retains 87% activity after treatment at 50°C, activity completely lost at 60°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. The soluble and active recombinant enzyme is expressed in the periplasmic space with the vector pET-22b
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Camargo Plessmann, E.; Silva, S.; Roitmann, I.; De Souza, W.; Jankevicius, J.V.; Dollet, M.
Enzymes of ornithine-arginine metabolism in trypanosomatids of the genus Phytomonas
J. Protozool.
34
439-441
1987
Euphorbia sp., Solanum lycopersicum, Manihot esculenta, Phytomonas davidi
-
brenda
Eichler, W.
L-Citrulline
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
8
412-418
1985
Homo sapiens, Tetrahymena sp.
-
brenda
Park, B.S.; Hirotani, A.; Nakano, Y.; Kitaoka, S.
Subcellular distribution and some properties of citrullinase in Euglena gracilis Z
Agric. Biol. Chem.
49
2205-2206
1985
Euglena gracilis, Tetrahymena sp.
-
brenda
Park, B.S.; Hirotani, A.; Nakano, Y.; Kitaoka, S.
The physiological role and catabolism of arginine in Euglena gracilis
Agric. Biol. Chem.
47
2561-2567
1983
Euglena gracilis
-
brenda
Hill, D.L.; Chambers, P.
The biosynthesis of proline by Tetrahymena pyriformis
Biochim. Biophys. Acta
148
435-447
1967
Tetrahymena sp.
brenda
Eichler, W.
Regulation of growth and polyamine biosynthesis of the ciliated protozoan Tetrahymena thermophila. Effects of L-arginine metabolites and polyamines
Biol. Chem. Hoppe-Seyler
371
273-282
1990
Tetrahymena sp.
brenda
Mahawar, M.; Kirimanjeswara, G.S.; Metzger, D.W.; Bakshi, C.S.
Contribution of citrulline ureidase to Francisella tularensis strain Schu S4 pathogenesis
J. Bacteriol.
191
4798-4806
2009
Francisella tularensis
brenda
Zhu, T.; Fang, S.; Wang, W.; Wang, K.; Cui, Z.; Wang, C.
The expression, purification and activity analysis of Francisella tularensis citrulline ureidase in Escherichia coli
J. Appl. Biomed.
13
189-194
2015
Francisella tularensis subsp. tularensis (Q5NHL7)
-
brenda
Timofeev, V.; Bakhteeva, I.; Pavlov, V.; Mokrievich, A.
Citrulline ureidase gene diversity in the genus Francisella
Mol. Gen. Mikrobiol. Virusol.
30
173-180
2015
no activity in Francisella tularensis ssp. holarctica
brenda
Sarva, S.T.; Waldo, R.H.; Belland, R.J.; Klose, K.E.
Comparative Transcriptional Analyses of Francisella tularensis and Francisella novicida
PLoS ONE
11
e0158631
2016
Francisella tularensis subsp. novicida, Francisella tularensis subsp. novicida U112, Francisella tularensis subsp. tularensis (Q5NHL7)
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