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Literature summary for 2.7.4.3 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)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8TZY2
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-

Purification (Commentary)

Purification (Comment) Organism
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Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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Synonyms

Synonyms Comment Organism
pfSMCnbd
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Pyrococcus furiosus
structural maintenance of chromosome protein
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Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
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assay at Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Pyrococcus furiosus