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

BRENDA support

Refine search

Search Crystallization (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 3 of 3
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.251crystal structure of PagP in an SDS /2-methyl-2,4-pentanediol cosolvent system, to 1.4 A resolution. Phospholipid access occurs at the crenel present between strands F and G
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.251molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.251solution NMR spectroscopy of PagP in both dodecylphosphocholine and n-octyl-beta-D-glucoside detergent micelles. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha-helix. The beta-barrel is well defined, whereas the loops connecting individual beta-strands show considerable mobility. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface. The active site of PagP is situated on the outer surface of the outer membrane
Results 1 - 3 of 3