S00432
type: Enzyme
rlcp: p450
cath: Metallo-beta-lactamase; Chain A
ec: https://purl.uniprot.org/enzyme/3.5.2.6
macie: M0016
uniprot: P04190
kegg enzyme: beta-lactamase
kegg enzyme: penicillinase
kegg enzyme: cephalosporinase
kegg enzyme: neutrapen
kegg enzyme: penicillin beta-lactamase
kegg enzyme: exopenicillinase
kegg enzyme: ampicillinase
kegg enzyme: penicillin amido-beta-lactamhydrolase
kegg enzyme: penicillinase I, II
kegg enzyme: beta-lactamase I-III
kegg enzyme: beta-lactamase A, B, C
kegg enzyme: beta-lactamase AME I
kegg enzyme: cephalosporin-beta-lactamase
kegg pathway: Penicillin and cephalosporin biosynthesis
kegg pathway: beta-Lactam resistance
kegg cofactor: Zinc
kegg substrate: beta-Lactam
kegg substrate: Penicillin
kegg substrate: Cephalosporin
kegg substrate: H2O
kegg product: Substituted beta-amino acid
pdb: 1bc2A
pdb: 1bc2B
pdb: 1bmcA
pdb: 1bmeA
pdb: 1bvtA
pdb: 1dxkA
pdb: 2bc2A
pdb: 2bc2B
pdb: 3bc2A
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1bc2A
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1bc2B
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1bmcA
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1bmeA
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1bvtA
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 1dxkA
pdb bound state: Unbound
  compound: beta-Lactam
  pdb: 2bc2A
references: An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35-nm resolution.
references: Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II.
references: The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
references: Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
references: Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.
references: Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase.
references: Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution.
references: 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.
references: X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
references: 1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus.
references: The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
references: Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
references: Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutions.
references: On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
references: Metallo-beta-lactamase: structure and mechanism.
references: 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.
references: Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
references: Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis.
references: Intermediate in beta-lactam hydrolysis catalyzed by a dinuclear zinc(II) complex: relevance to the mechanism of metallo-beta-lactamase.
references: Novel mechanism of hydrolysis of therapeutic beta-lactams by Stenotrophomonas maltophilia L1 metallo-beta-lactamase.
references: Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus.
references: Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding.
references: 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.
references: Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus complexed with benzylpenicillin and a quantum chemical study of the reaction mechanism.
references: Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection.
references: Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.
references: Insights into the structure and dynamics of the dinuclear zinc beta-lactamase site from Bacteroides fragilis.
references: Structural determinants and hydrogen-bond network of the mononuclear zinc(II)-beta-lactamase active site.
references: Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem.
references: 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.
references: Biochemical characterization of the acquired metallo-beta-lactamase SPM-1 from Pseudomonas aeruginosa.
references: Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases.
references: Zinc-bound thiolate-disulfide exchange: a strategy for inhibiting metallo-beta-lactamases.
references: The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril.
references: The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.
references: Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations.
comment: 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 this 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 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. frag…

Metallo-beta-lactamase; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.60.15.10
catalytic domain: index.html

Penicillin and cephalosporin biosynthesis
type: KeggPathway
references: KEGG:MAP00311

beta-Lactam resistance
type: KeggPathway
references: KEGG:MAP00312

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

beta-Lactam
type: KeggSubstrate
references: KEGG:C01866
compound type: amide group

Penicillin
type: KeggSubstrate
references: KEGG:C00395
compound type: carboxyl group
compound type: peptide/protein
compound type: sulfide group

Cephalosporin
type: KeggSubstrate
references: KEGG:C00875
compound type: amide group
compound type: amine group
compound type: carboxyl group
compound type: sulfide group

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Substituted beta-amino acid
type: KeggProduct
references: KEGG:C03806
compound type: amino acids

1bc2A
type: Pdb
references: 1bc2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bc2
catalytic residue: ;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88;ASP 90;HIS 149;CYS 168;HIS 210(two Zinc binding)

1bc2B
type: Pdb
references: 1bc2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bc2
catalytic residue: ;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88;ASP 90;HIS 149;CYS 168;HIS 210(two Zinc binding)

1bmcA
type: Pdb
references: 1bmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bmc
catalytic residue: ASP 90;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88; ;HIS 149; ;HIS 210(Zinc binding)

1bmeA
type: Pdb
references: 1bme
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bme
catalytic residue: ;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88;ASP 90;HIS 149;CYS 168;HIS 210(two Zinc binding)

1bvtA
type: Pdb
references: 1bvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvt
catalytic residue: ;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88;ASP 90;HIS 149;CYS 168;HIS 210(two Zinc binding)

1dxkA
type: Pdb
references: 1dxk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxk
catalytic residue: ASP 90;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88; ;HIS 149; ;HIS 210(Zinc binding)
comment: mutant C168S

2bc2A
type: Pdb
references: 2bc2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bc2
catalytic residue: ASP 90;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88; ;HIS 149; ;HIS 210(Zinc binding)
comment: mutant C168CSD

2bc2B
type: Pdb
references: 2bc2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bc2
catalytic residue: ASP 90;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88; ;HIS 149; ;HIS 210(Zinc binding)
comment: mutant C168CSD

3bc2A
type: Pdb
references: 3bc2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3bc2
catalytic residue: ASP 90;ASN 180
cofactor binding residue: ASP 56;HIS 86;HIS 88; ;HIS 149; ;HIS 210(Zinc binding)
comment: mutant C168CSD

An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35-nm resolution.
type: BibliographicResource
comment: X-ray crystallography (3.5 Angstroms)
medline id: 88133841
references: http://www.ncbi.nlm.nih.gov/pubmed/3124808
journal: Biochem J
volume: 248
pages: 181-8
published year: 1987
authors:
  item: Sutton B.J.
  item: Artymiuk P.J.
  item: Cordero-Borboa A.E.
  item: Little C.
  item: Phillips D.C.
  item: Waley S.G

Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2501295
journal: J Biol Chem
volume: 264
pages: 11682-7
published year: 1989
authors:
  item: Lim HM
  item: Pene JJ

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
type: BibliographicResource
comment: X-ray crystallography (2.5 Angstroms)
medline id: 96067120
references: http://www.ncbi.nlm.nih.gov/pubmed/7588620
journal: EMBO J
volume: 14
pages: 4914-21
published year: 1995
authors:
  item: Carfi A
  item: Pares S
  item: Duee E
  item: Galleni M
  item: Duez C
  item: Frere JM
  item: Dideberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
type: BibliographicResource
comment: X-ray crystallography (1.85 Angstroms)
medline id: 96434328
references: http://www.ncbi.nlm.nih.gov/pubmed/8805566
journal: Structure
volume: 4
pages: 823-36
published year: 1996
authors:
  item: Concha NO
  item: Rasmussen BA
  item: Bush K
  item: Herzberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.
type: BibliographicResource
comment: X-ray crystallography (Cd(2+)-bound;2.1 Angstroms, Hg(2+)-soaked zinc-containing;2.7 Angstroms)
medline id: 98078582
references: http://www.ncbi.nlm.nih.gov/pubmed/9416622
journal: Protein Sci
volume: 6
pages: 2671-6
published year: 1997
authors:
  item: Concha NO
  item: Rasmussen BA
  item: Bush K
  item: Herzberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase.
type: BibliographicResource
comment: X-ray crystallography (complex with potent inhibitors)
references: http://www.ncbi.nlm.nih.gov/pubmed/9545432
journal: Chem Biol
volume: 5
pages: 185-96
published year: 1998
authors:
  item: Toney JH
  item: Fitzgerald PM
  item: Grover-Sharma N
  item: Olson SH
  item: May WJ
  item: Sundelof JG
  item: Vanderwall DE
  item: Cleary KA
  item: Grant SK
  item: Wu JK
  item: Kozarich JW
  item: Pompliano DL
  item: Hammond GG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution.
type: BibliographicResource
comment: X-ray crystallography (1.85 Angstroms)
medline id: 98244858
references: http://www.ncbi.nlm.nih.gov/pubmed/9578564
journal: Biochemistry
volume: 37
pages: 6791-800
published year: 1998
authors:
  item: Fitzgerald PM
  item: Wu JK
  item: Toney JH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

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.
type: BibliographicResource
comment: X-ray crystallography (1.9 Angstroms)
medline id: 98400945
references: http://www.ncbi.nlm.nih.gov/pubmed/9730812
journal: Biochemistry
volume: 37
pages: 12404-11
published year: 1998
authors:
  item: Fabiane SM
  item: Sohi MK
  item: Wan T
  item: Payne DJ
  item: Bateson JH
  item: Mitchell T
  item: Sutton BJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
type: BibliographicResource
comment: X-ray crystallography (2.0 Angstroms, orthorhombic crystal form)
references: http://www.ncbi.nlm.nih.gov/pubmed/9761816
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 45-57
published year: 1998
authors:
  item: Carfi A
  item: Duee E
  item: Paul-Soto R
  item: Galleni M
  item: Frere JM
  item: Dideberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus.
type: BibliographicResource
comment: X-ray crystallography (1.85 Angstroms)
medline id: 98437525
references: http://www.ncbi.nlm.nih.gov/pubmed/9761898
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 313-23
published year: 1998
authors:
  item: Carfi A
  item: Duee E
  item: Galleni M
  item: Frere JM
  item: Dideberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
type: BibliographicResource
comment: X-ray crystallography (1.7 Angstroms)
medline id: 99030465
references: http://www.ncbi.nlm.nih.gov/pubmed/9811546
journal: J Mol Biol
volume: 284
pages: 125-36
published year: 1998
authors:
  item: Ullah JH
  item: Walsh TR
  item: Taylor IA
  item: Emery DC
  item: Verma CS
  item: Gamblin SJ
  item: Spencer J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
type: BibliographicResource
comment: X-ray crystallography (2.6 Angstroms, active site mutation)
medline id: 99224909
references: http://www.ncbi.nlm.nih.gov/pubmed/10210203
journal: Protein Sci
volume: 8
pages: 249-52
published year: 1999
authors:
  item: Li Z
  item: Rasmussen BA
  item: Herzberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10336469
journal: J Biol Chem
volume: 274
pages: 15706-11
published year: 1999
authors:
  item: Yang Y
  item: Keeney D
  item: Tang X
  item: Canfield N
  item: Rasmussen BA

On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10433708
journal: Biochemistry
volume: 38
pages: 10013-23
published year: 1999
authors:
  item: Wang Z
  item: Fast W
  item: Benkovic SJ

Metallo-beta-lactamase: structure and mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10508665
journal: Curr Opin Chem Biol
volume: 3
pages: 614-22
published year: 1999
authors:
  item: Wang Z
  item: Fast W
  item: Valentine AM
  item: Benkovic SJ

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.
type: BibliographicResource
comment: X-ray crystallography (native;3.1 Angstroms, complex with inhibitor;2.0 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/10757977
journal: Biochemistry
volume: 39
pages: 4288-98
published year: 2000
authors:
  item: Concha NO
  item: Janson CA
  item: Rowling P
  item: Pearson S
  item: Cheever CA
  item: Clarke BP
  item: Lewis C
  item: Galleni M
  item: Frere JM
  item: Payne DJ
  item: Bateson JH
  item: Abdel-Meguid SS
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
type: BibliographicResource
comment: X-ray crystallography (1.85 Angstroms, active site mutation)
medline id: 20386639
references: http://www.ncbi.nlm.nih.gov/pubmed/10933508
journal: Protein Sci
volume: 9
pages: 1402-6
published year: 2000
authors:
  item: Chantalat L
  item: Duee E
  item: Galleni M
  item: Frere JM
  item: Dideberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11327823
journal: Biochemistry
volume: 40
pages: 1640-50
published year: 2001
authors:
  item: Fast W
  item: Wang Z
  item: Benkovic SJ

Intermediate in beta-lactam hydrolysis catalyzed by a dinuclear zinc(II) complex: relevance to the mechanism of metallo-beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11439042
journal: J Am Chem Soc
volume: 123
pages: 6555-63
published year: 2001
authors:
  item: Kaminskaia NV
  item: Spingler B
  item: Lippard SJ

Novel mechanism of hydrolysis of therapeutic beta-lactams by Stenotrophomonas maltophilia L1 metallo-beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11443136
journal: J Biol Chem
volume: 276
pages: 33638-44
published year: 2001
authors:
  item: Spencer J
  item: Clarke AR
  item: Walsh TR

Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11457108
journal: J Am Chem Soc
volume: 123
pages: 3759-70
published year: 2001
authors:
  item: Suarez D
  item: Merz KM Jr

Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11484222
journal: Proteins
volume: 44
pages: 448-59
published year: 2001
authors:
  item: Salsbury FR Jr
  item: Crowley MF
  item: Brooks CL 3rd

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.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11551939
journal: J Biol Chem
volume: 276
pages: 45065-78
published year: 2001
authors:
  item: de Seny D
  item: Heinz U
  item: Wommer S
  item: Kiefer M
  item: Meyer-Klaucke W
  item: Galleni M
  item: Frere JM
  item: Bauer R
  item: Adolph HW

Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus complexed with benzylpenicillin and a quantum chemical study of the reaction mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11583551
journal: J Am Chem Soc
volume: 123
pages: 9867-79
published year: 2001
authors:
  item: Diaz N
  item: Suarez D
  item: Merz KM Jr

Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection.
type: BibliographicResource
comment: Identification of critical residues
references: http://www.ncbi.nlm.nih.gov/pubmed/11714924
journal: Protein Sci
volume: 10
pages: 2556-65
published year: 2001
authors:
  item: Materon IC
  item: Palzkill T

Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.
type: BibliographicResource
comment: Metal site
references: http://www.ncbi.nlm.nih.gov/pubmed/11847294
journal: Protein Sci
volume: 11
pages: 707-12
published year: 2002
authors:
  item: Gomes CM
  item: Frazao C
  item: Xavier AV
  item: Legall J
  item: Teixeira M

Insights into the structure and dynamics of the dinuclear zinc beta-lactamase site from Bacteroides fragilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12022865
journal: Biochemistry
volume: 41
pages: 6615-30
published year: 2002
authors:
  item: Suarez D
  item: Brothers EN
  item: Merz KM Jr

Structural determinants and hydrogen-bond network of the mononuclear zinc(II)-beta-lactamase active site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12203007
journal: J Biol Inorg Chem
volume: 7
pages: 704-12
published year: 2002
authors:
  item: Dal Peraro M
  item: Vila AJ
  item: Carloni P

Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12395427
journal: J Comput Chem
volume: 23
pages: 1587-600
published year: 2002
authors:
  item: Suarez D
  item: Diaz N
  item: Merz KM Jr

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.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12507470
journal: J Mol Biol
volume: 325
pages: 651-60
published year: 2003
authors:
  item: Garcia-Saez I
  item: Mercuri PS
  item: Papamicael C
  item: Kahn R
  item: Frere JM
  item: Galleni M
  item: Rossolini GM
  item: Dideberg O

Biochemical characterization of the acquired metallo-beta-lactamase SPM-1 from Pseudomonas aeruginosa.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12543663
journal: Antimicrob Agents Chemother
volume: 47
pages: 582-7
published year: 2003
authors:
  item: Murphy TA
  item: Simm AM
  item: Toleman MA
  item: Jones RN
  item: Walsh TR

Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12578382
journal: Biochemistry
volume: 42
pages: 1673-83
published year: 2003
authors:
  item: Siemann S
  item: Clarke AJ
  item: Viswanatha T
  item: Dmitrienko GI

Zinc-bound thiolate-disulfide exchange: a strategy for inhibiting metallo-beta-lactamases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12611529
journal: Inorg Chem
volume: 42
pages: 1604-15
published year: 2003
authors:
  item: Boerzel H
  item: Koeckert M
  item: Bu W
  item: Spingler B
  item: Lippard SJ

The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12684522
journal: J Biol Chem
volume: 278
pages: 23868-73
published year: 2003
authors:
  item: Garcia-Saez I
  item: Hopkins J
  item: Papamicael C
  item: Franceschini N
  item: Amicosante G
  item: Rossolini GM
  item: Galleni M
  item: Frere JM
  item: Dideberg O

The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12724330
journal: J Biol Chem
volume: 278
pages: 29240-51
published year: 2003
authors:
  item: Damblon C
  item: Jensen M
  item: Ababou A
  item: Barsukov I
  item: Papamicael C
  item: Schofield CJ
  item: Olsen L
  item: Bauer R
  item: Roberts GC

Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12826725
journal: Protein Eng
volume: 16
pages: 341-50
published year: 2003
authors:
  item: Oelschlaeger P
  item: Schmid RD
  item: Pleiss J

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.4917-4920

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.831-832

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.1
reference step: 2

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.12408-12410, Fig.7

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.55-57

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.322

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.7, p.130-133
reference step: 2

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme 5, p.10020-10022
reference step: 2

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.6, Fig.7, p.618-620

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.1403-1405

ReferenceForCatalyticMechanism
reference index: 21
reference section: p.1599

ReferenceForCatalyticMechanism
reference index: 24
reference section: Scheme 4
reference step: 1

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.710-711

ReferenceForCatalyticMechanism
reference index: 30
reference section: Fig.6, p.656