Literature summary for 3.5.2.6 extracted from

Borra, P.S.; Leiros, H.K.; Ahmad, R.; Spencer, J.; Leiros, I.; Walsh, T.R.; Sundsfjord, A.; Samuelsen, O.
Structural and computational investigations of VIM-7: insights into the substrate specificity of vim metallo-beta-lactamases (2011), J. Mol. Biol., 411, 174-189.

Crystallization (Commentary)

Crystallization (Comment)	Organism
as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 6066, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 6066, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224

Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	enzyme has a a fourcoordinate Zn2 site and both tetrahedral and pentacoordinated Zn1 sites	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q840P9	-	-

Synonyms

Synonyms	Comment	Organism
VIM-7	-	Pseudomonas aeruginosa

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)