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

BRENDA support

Literature summary extracted from

  • Riise, E.K.; Lorentzen, M.S.; Helland, R.; Smalas, A.O.; Leiros, H.K.; Willassen, N.P.
    The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 A reveals structural aspects of cold adaptation (2007), Acta Crystallogr. Sect. D, 63, 135-148.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.6 comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability Proteus mirabilis
1.11.1.6 diffraction to 1.96 A. Comparison with catalase from Proteus mirabilis. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. The reduced thermal stability of cold-adapted Aliivibrio salmonicida catalase may be explained by a reduced number of ion-pair networks and displacement of the four C-terminal alpha-helices Aliivibrio salmonicida LFI1238

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.6 Aliivibrio salmonicida LFI1238 Q3LSM1
-
-
1.11.1.6 Proteus mirabilis P42321
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.6 heme
-
 Aliivibrio salmonicida LFI1238
1.11.1.6 heme
-
 Proteus mirabilis