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Literature summary extracted from

  • Sundaresan, R.; Ebihara, A.; Kuramitsu, S.; Yokoyama, S.; Kumarevel, T.; Ponnuraj, K.
    Crystal structure analysis of ornithine transcarbamylase from Thermus thermophilus - HB8 provides insights on the plasticity of the active site (2015), Biochem. Biophys. Res. Commun., 465, 174-179.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.3 gene argF Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.3 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 Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.3 carbamoyl phosphate + L-ornithine Thermus thermophilus
-
 phosphate + L-citrulline
-
 ?
2.1.3.3 carbamoyl phosphate + L-ornithine Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 phosphate + L-citrulline
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.3 Thermus thermophilus Q5SJ15 gene argF
-
2.1.3.3 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SJ15 gene argF
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.3 carbamoyl phosphate + L-ornithine
-
 Thermus thermophilus phosphate + L-citrulline
-
 ?
2.1.3.3 carbamoyl phosphate + L-ornithine
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 phosphate + L-citrulline
-
 ?
2.1.3.3 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 Thermus thermophilus ?
-
 ?
2.1.3.3 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 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.3.3 aTtOTCase
-
 Thermus thermophilus
2.1.3.3 ornithine transcarbamylase
-
 Thermus thermophilus
2.1.3.3 otcase
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
2.1.3.3 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 Thermus thermophilus