Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Neelon, K.; Schreier, H.J.; Meekins, H.; Robinson, P.M.; Roberts, M.F.
    Compatible solute effects on thermostability of glutamine synthetase and aspartate transcarbamoylase from Methanococcus jannaschii (2005), Biochim. Biophys. Acta, 1753, 164-173.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.2 expression in Escherichia coli Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Escherichia coli
-
-
-
2.1.3.2 Methanocaldococcus jannaschii
-
-
-
6.3.1.2 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.2 recombinant enzyme Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.2 carbamoyl phosphate + L-aspartate
-
Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
?
2.1.3.2 carbamoyl phosphate + L-aspartate
-
Methanocaldococcus jannaschii phosphate + N-carbamoyl-L-aspartate
-
?

Subunits

EC Number Subunits Comment Organism
2.1.3.2 trimer
-
Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 aspartate transcarbamoylase
-
Escherichia coli
2.1.3.2 aspartate transcarbamoylase
-
Methanocaldococcus jannaschii
2.1.3.2 ATCase
-
Escherichia coli
2.1.3.2 ATCase
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.2 37
-
assay at Escherichia coli
2.1.3.2 55
-
assay at Methanocaldococcus jannaschii
6.3.1.2 55
-
-
Methanocaldococcus jannaschii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.3.1.2 40 70 about 50% of maximal activity at 40°C and at 70°C Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.3.2 55 65 4 min, loss of 70% of secondary structure in absence of solutes, Tm is highly enhanced in presence of KCl, NaCl, or alpha and beta isomers of K+-glutamate, NaCl, KCl, glycine, and betaine are not thermoprotective, but trehalose, sucrose, and K+-glutamate are, K+-glutamate raises Tm and maintains enzyme activity, overview Escherichia coli
2.1.3.2 95
-
30 min, stable in solutes, but large loss of secondary structure in absence of solutes, the loss is enhanced in presence of KCl, NaCl, or K+-glutamate, glycine and sucrose are thermoprotective Methanocaldococcus jannaschii
2.1.3.2 100
-
30 min, stable in solutes, but loss of 41% of secondary structure in absence of solutes, the loss is enhanced in presence of KCl, NaCl, or K+-glutamate, glycine and sucrose are thermoprotective Methanocaldococcus jannaschii
6.3.1.2 57
-
midpoint temperature of pure enzyme, none of the small molecules tested significantly stabilizes the enzyme. Stabilization by Escherichia coli GroEL or ribosomal protein L2. Protein-protein interactions appear to be the dominant factor in stabilizing the archael enzyme at the growth temperature (85°C) Methanocaldococcus jannaschii