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Literature summary extracted from

  • Nishitani, Y.; Aono, R.; Nakamura, A.; Sato, T.; Atomi, H.; Imanaka, T.; Miki, K.
    Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization (2013), J. Mol. Biol., 425, 2709-2721.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.57 hanging-drop vapor diffusion method at 20°C. Crystal structures of the enzyme, in the apo-form and in complex with substrates Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.57 DELTAN1-84 mutant enzyme lacking the N-terminal 22 residues aggregates at 75°C Thermococcus kodakarensis
2.4.2.57 additional information all the mutants, forming smaller assemblies, display a decrease in thermostability compared to the wild-type enzyme. Tk-AMPpaseDELTAC10 aggregates at temperatures of 80°C or higher, while aggregation of Tk-AMPpaseDELTAN84 is observed at 75°C and that of Tk-AMPpase?N84DELTAC10 is observed at 70°C Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.57 Thermococcus kodakarensis Q5JCX3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.57
-
 Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.57 2.94
-
 60°C, pH not specified in the publication Thermococcus kodakarensis
2.4.2.57 14.69
-
 85°C, pH not specified in the publication Thermococcus kodakarensis

Subunits

EC Number Subunits Comment Organism
2.4.2.57 multimer forms a large macromolecular structure of more than 40 subunits in solution. Structures of two truncated forms of Tk-AMPpase (Tk-AMPpaseDELTAN84 and Tk-AMPpaseDELTAC10) clarify that the multimerization is achieved by two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain, which consists of an unexpected domain-swapping interaction. The N-terminal domain, characteristic of archaeal enzymes, is essential for enzymatic activity, participating in multimerization as well as domain closure of the active site upon substrate binding. Biochemical analysis demonstrates that the macromolecular assembly of the enzyme contributes to its high thermostability Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
2.4.2.57 AMPpase
-
 Thermococcus kodakarensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.2.57 additional information
-
 the macromolecular assembly of the enzyme contributes to its high thermostability Thermococcus kodakarensis