Why Urease Is a Di-Nickel Enzyme whereas the CcrA β-Lactamase Is a Di-Zinc Enzyme

2012 ◽  
Vol 116 (35) ◽  
pp. 10649-10656 ◽  
Author(s):  
Crystal E. Valdez ◽  
Anastassia N. Alexandrova
Keyword(s):  
Zinc Enzyme ◽  
Nickel Enzyme

Theoretical Investigation of the Reaction Mechanism of the Dinuclear Zinc Enzyme Dihydroorotase

2008 ◽  
Vol 14 (14) ◽  
pp. 4287-4292 ◽  
Author(s):  
Rong-Zhen Liao ◽  
Jian-Guo Yu ◽  
Frank M. Raushel ◽  
Fahmi Himo
Keyword(s):  
Reaction Mechanism ◽  
Theoretical Investigation ◽  
Zinc Enzyme

The Impact of pH on Catalytically Critical Protein Conformational Changes: The Case of the Urease, a Nickel Enzyme

2019 ◽  
Vol 25 (52) ◽  
pp. 12145-12158 ◽  
Author(s):  
Luca Mazzei ◽  
Michele Cianci ◽  
Stefano Benini ◽  
Stefano Ciurli
Keyword(s):  
Conformational Changes ◽  
Protein Conformational Changes ◽  
Nickel Enzyme ◽  
The Impact

Macrocyclic Zinc(II) Complexes for Selective Recognition of Nucleobases in Single- and Double-Stranded Polynucleotides

2000 ◽  
Vol 25 (1) ◽  
pp. 1-64 ◽  
Author(s):  
Eiichi Kimura ◽  
Emiko Kikuta
Keyword(s):  
Antimicrobial Activities ◽  
Biological Properties ◽  
Transcriptional Factor ◽  
Selective Recognition ◽  
Intrinsic Properties ◽  
Dna Footprinting ◽  
Double Stranded Dna ◽  
Zinc Enzyme ◽  
Model Study ◽  
Basic Understanding

The model study of zinc enzyme by Zn2+–cyclen complexes (cyclen = 1, 4, 7, 10-tetraazacyclododecane) disclosed the intrinsic properties of zinc(II) as having strong anion affinities and yet the resulting Zn2+–anion bonds have a labile nature. The basic understanding has evolved into novel selective nucleobase recognition by the Zn2+–cyclen complexes. The Zn2+–aromatic pendant cyclen complexes selectively and effectively bind to thymine T (or uracil U) in single- and double-stranded DNA (or RNA). The Zn2+ complexes work like molecular zippers to break A–T pairs in double-stranded DNA, as proven by various physicochemical and DNA footprinting measurements. Moreover, these Zn2+–complexes affect relevant biochemical and ultimately biological properties such as inhibition of a transcriptional factor and antimicrobial activities.

Zinc enzyme modelling with zinc complexes of polar pyrazolylborate ligands

2007 ◽  
Vol 360 (5) ◽  
pp. 1510-1516 ◽  
Author(s):  
C. Pérez Olmo ◽  
K. Böhmerle ◽  
H. Vahrenkamp
Keyword(s):  
Zinc Complexes ◽  
Zinc Enzyme

Modeling Zinc Enzyme Inhibition with Functional Thiolate Ligands

2006 ◽  
Vol 45 (26) ◽  
pp. 10799-10806 ◽  
Author(s):  
Teame Tekeste ◽  
Heinrich Vahrenkamp
Keyword(s):  
Enzyme Inhibition ◽  
Thiolate Ligands ◽  
Zinc Enzyme

scholarly journals The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275

1985 ◽  
Vol 229 (3) ◽  
pp. 791-797 ◽  
Author(s):  
R Bicknell ◽  
E L Emanuel ◽  
J Gagnon ◽  
S G Waley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
The Other ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Zinc Enzyme ◽  
Pseudomonas Maltophilia ◽  
Measurable Rate ◽  
Beta Lactamase Ii

The production and purification of a tetrameric zinc beta-lactamase from Pseudomonas maltophilia IID 1275 were greatly improved. Three charge variants were isolated by chromatofocusing. The subunits each contain two atomic proportions of zinc and (in two of the variants) one residue of cysteine. The thiol group is not required for activity, nor does it appear to bind to the metal. Replacement of zinc by cobalt, cadmium or nickel takes place at a measurable rate, and gives enzymes that are less active than the zinc enzyme. The properties of this enzyme differ from those of the other known zinc beta-lactamase, beta-lactamase II from Bacillus cereus. The amino acid sequence of the N-terminal 32 residues was determined; there is no similarity to the N-terminal sequences of other beta-lactamases.

scholarly journals Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme

FEBS Journal ◽  
2011 ◽  
Vol 278 (8) ◽  
pp. 1252-1263 ◽  
Author(s):  
Louise E. Horsfall ◽  
Youssef Izougarhane ◽  
Patricia Lassaux ◽  
Nathalie Selevsek ◽  
Benoit M. R. Liénard ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Resistance Profile ◽  
Antibiotic Resistance Profile ◽  
Zinc Enzyme
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