Penicillin and cephalosporin biosynthesis
ASP 52;HIS 82;HIS 84;ASP 86;HIS 145;CYS 164;HIS 206(Two zinc binding)
ASP 69;HIS 99;HIS 101;ASP 103;HIS 162;CYS 181;HIS 223(Two zinc binding)
ASP 69;HIS 99;HIS 101;ASP 103;HIS 162; ;HIS 223(Two zinc binding)
ASP 48;HIS 77;HIS 79;ASP 81;HIS 139;CYS 158;HIS 197(Two zinc binding)
ASP 53;HIS 84;HIS 86;ASP 88;HIS 160;ASP 184;HIS 225(Two zinc binding)
Insights into the structure and dynamics of the dinuclear zinc beta-lactamase site from Bacteroides fragilis.
An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35-nm resolution.
Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II.
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
X-ray crystallography (Cd(2+)-bound;2.1 Angstroms, Hg(2+)-soaked zinc-containing;2.7 Angstroms)
Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.
X-ray crystallography (complex with potent inhibitors)
Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase.
Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution.
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
X-ray crystallography (2.0 Angstroms, orthorhombic crystal form)
X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus.
The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
X-ray crystallography (2.6 Angstroms, active site mutation)
Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutions.
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
Metallo-beta-lactamase: structure and mechanism.
X-ray crystallography (native;3.1 Angstroms, complex with inhibitor;2.0 Angstroms)
Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
X-ray crystallography (1.85 Angstroms, active site mutation)
Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis.
Intermediate in beta-lactam hydrolysis catalyzed by a dinuclear zinc(II) complex: relevance to the mechanism of metallo-beta-lactamase.
Novel mechanism of hydrolysis of therapeutic beta-lactams by Stenotrophomonas maltophilia L1 metallo-beta-lactamase.
Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus.
Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding.
Metal ion binding and coordination geometry for wild type and mutants of metallo-beta -lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach.
Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus complexed with benzylpenicillin and a quantum chemical study of the reaction mechanism.
Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection.
Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.
Structural determinants and hydrogen-bond network of the mononuclear zinc(II)-beta-lactamase active site.
Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem.
Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.
Biochemical characterization of the acquired metallo-beta-lactamase SPM-1 from Pseudomonas aeruginosa.
Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases.
Zinc-bound thiolate-disulfide exchange: a strategy for inhibiting metallo-beta-lactamases.
The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril.
The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.
Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations.
This enzyme belongs to the class-B beta-lactamase (metallo-beta-lactamase) family. According to the literature [9] & [15], there are three types of metallo-beta-lactamases. (1) Enzyme from B. cereus: active with one zinc ion, and the binding of the second zinc increases its activity. (2) Enzyme from B. fragilis: active with two zinc ion. (3) Enzyme from A. hydrophilia: active with one zinc ion, and inhibited by the second zinc ion. Thus, the catalytic mechanism of the monozinc form is different from that of the dizinc form. According to the literature [3] & [15], the catalytic mechanism of the monozinc enzyme (S00432) is proposed as follows: (a) Zinc pre-forms the nucleophilic hydroxide, in combination with Asp90. (b) Zinc-bound hydroxide acts as a nucleophile to attack the carbonyl carbon, leading to a dianionic tetrahedral intermediate. (c) Zinc stabilizes the oxyanion of the dianionic intermediate, along with Asn180. (d) Asp90 deprotonates the anionic intermediate, to yield a dianionic tetrahedral intermediate, as a general base. (e) The breakdown of the dianionic tetrahedral intermediate is facilitated by protonation from Asp90 as a general acid. On the other hand, according to the literature [14] & [15], the catalytic mechanism of this dizinc enzyme (S00515) is as follows: (a) Zn1-bound hydroxide acts as a nucleophile to attack the carbonyl carbon. (b) Cleavage of the C-N bond results in a negatively charged nitrogen leaving group. (c) Asn193 stabilizes the carbonyl oxygen, together with Zn1. (d) Zn2 stabilizes the negatively charged leaving group, acting as a superacid. (e) Protonation of the negatively charged nitrogen by a second water molecule from solvent leads to the breakdown of the intermediate. (This protonation prior to the C-N bond cleavage is not required.) The paper [9] suggested that there had been an evolutionary pathway from a monozinc enzyme (A. hydrophilia) through an enzyme with one or two zinc ions (B. cereus: S00432) to a dizinc enzyme (B. fragilis: S00515).