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

BRENDA support

Literature summary for 4.3.2.2 extracted from

  • Toth, E.A.; Worby, C.; Dixon, J.E.; Goedken, E.R.; Marqusee, S.; Yeates, T.O.
    The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds (2000), J. Mol. Biol., 301, 433-450.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure is determined to 2.1 resolution. Hanging drop vapor diffusion method at 18°C Pyrobaculum aerophilum

General Stability

General Stability Organism
the structure of adenylosuccinate lyase reveals that this protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation Pyrobaculum aerophilum

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
Pyrobaculum aerophilum 5622
-

Organism

Organism UniProt Comment Textmining
Pyrobaculum aerophilum Q8ZY28
-
-
Pyrobaculum aerophilum DSM 7523 Q8ZY28
-
-

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Pyrobaculum aerophilum