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Literature summary for 2.1.3.3 extracted from

  • Polo, L.M.; Gil-Ortiz, F.; Cantin, A.; Rubio, V.
    New insight into the transcarbamylase family: the structure of putrescine transcarbamylase, a key catalyst for fermentative utilization of agmatine (2012), PLoS ONE, 7, e31528.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
enzyme protomer structure, overview Enterococcus faecalis

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Enterococcus faecalis

Protein Variants

Protein Variants Comment Organism
additional information confirmation of decreased stability of the trimer of the enzyme lacking the C-terminal helix by deleting this helix Enterococcus faecalis
R54G site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity Enterococcus faecalis
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 Enterococcus faecalis

Inhibitors

Inhibitors Comment Organism Structure
delta-N-(phosphonoacetyl)-L-ornithine bisubstrate analogue inhibitor Enterococcus faecalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
32
-
L-ornithine recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C Enterococcus faecalis
36.4
-
L-ornithine recombinant wild-type enzyme, pH 8.5, 37°C Enterococcus faecalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120300
-
trimeric enzyme, gel filtration Enterococcus faecalis
230000
-
hexameric enzyme, gel filtration Enterococcus faecalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carbamoyl phosphate + L-ornithine Enterococcus faecalis
-
L-citrulline + phosphate
-
r

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis Q837U7
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
24
-
recombinant wild-type enzyme, substrate L-ornithine, pH 8.5, 37°C Enterococcus faecalis
82
-
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, substrate L-ornithine, pH 8.5, 37°C Enterococcus faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-ornithine
-
Enterococcus faecalis L-citrulline + phosphate
-
r
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 Enterococcus faecalis ?
-
?

Subunits

Subunits Comment Organism
hexamer two trimer structure Enterococcus faecalis
More presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview Enterococcus faecalis

Synonyms

Synonyms Comment Organism
ornithine transcarbamylase
-
Enterococcus faecalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Enterococcus faecalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Enterococcus faecalis

General Information

General Information Comment Organism
additional information sequence 230YGLY233 is the putrescine signature sequence Enterococcus faecalis
physiological function the OTC activity of the enzyme is involved in arginine biosynthesis Enterococcus faecalis