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

BRENDA support

Literature summary for 3.5.2.6 extracted from

  • Wang, J.; Palzkill, T.; Chow, D.
    Structural insight into the kinetics and DELTACp of interactions between TEM-1 beta-lactamase and beta-lactamase inhibitory protein (BLIP) (2009), J. Biol. Chem., 284, 595-609.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.2.6

Crystallization (Commentary)

Crystallization (Comment) Organism
microseeding, enzyme/beta-lactamase inhibitory protein(BLIP) complexes: BLIP/TEM-1, BLIP(W150A)/TEM-1 and BLIP(Y51A)/TEM-1 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
beta-lactamase inhibitory protein i.e. BLIP. Structures of two thermodynamically distinctive complexes of BLIP mutants with TEM-1 beta-lactamase. The complex BLIP Y51ATEM-1 is a tight binding complex with the most negative binding heat capacity change among all of the mutants, whereas BLIP W150ATEM-1 is a weak complex with one of the least negative binding heat capacity changes. BLIP Tyr51 is a canonical and Trp150 an anti-canonical TEM-1-contact residue (canonical refers to the alanine substitution resulting in a matched change in the hydrophobicity of binding free energy). Structure determination indicates a rearrangement of the interactions between Asp49 of the W150A BLIP mutant and the catalytic pocket of TEM-1. The Asp49 of W150A moves more than 4 A to form two new hydrogen bonds while losing four original hydrogen bonds Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P62593 containing the TEM-1 beta-lactamase expression plasmid DNA
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
TEM-1 beta-lactamase
-
 Escherichia coli