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Literature summary extracted from

  • Lammens, A.; Hopfner, K.
    Structural basis for adenylate kinase activity in ABC ATPases (2010), J. Mol. Biol., 401, 265-273 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.3 crystal structure of the nucleotide-binding domain of the Pyrococcus furiosus structural maintenance of chromosome protein (pfSMCnbd) in complex with the adenylate kinase inhibitor P1,P5-di(adenosine-5')pentaphosphate Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.3 Pyrococcus furiosus Q8TZY2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.3
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.3 2 ADP pfSMCnbd possesses reverse adenylate kinase activity. In adenylate kinase reactions, ATP binds to its canonical binding site while AMP binds to the Q-loop glutamine and a hydration water of the Mg2+ ion. Furthermore, mutational analysis indicates that adenylate kinase reaction occurs in the engaged pfSMCnbd dimer and requires the Signature motif for phosphate transfer Pyrococcus furiosus ATP + AMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.3 pfSMCnbd
-
 Pyrococcus furiosus
2.7.4.3 structural maintenance of chromosome protein
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.3 55
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.3 7.5
-
 assay at Pyrococcus furiosus