S00512
type: Enzyme
rlcp: p16
cath: Beta-lactamase
ec: https://purl.uniprot.org/enzyme/3.5.2.6
csa: 2blt
uniprot: P05364
uniprot: P00811
uniprot: Q46041
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 pathway: Penicillin and cephalosporin biosynthesis
kegg pathway: beta-Lactam resistance
kegg substrate: beta-Lactam
kegg substrate: Penicillin
kegg substrate: Cephalosporin
kegg substrate: H2O
kegg product: Substituted beta-amino acid
pdb: 1blsA
pdb: 1blsB
pdb: 1gceA
pdb: 1c3bA
pdb: 1c3bB
pdb: 1fcmA
pdb: 1fcmB
pdb: 1fcnA
pdb: 1fcnB
pdb: 1fcoA
pdb: 1fcoB
pdb: 1fswA
pdb: 1fswB
pdb: 1fsyA
pdb: 1fsyB
pdb: 2blsA
pdb: 2blsB
pdb: 2bltA
pdb: 2bltB
pdb: 3blsA
pdb: 3blsB
pdb: 1fr1A
pdb: 1fr1B
pdb: 1fr6A
pdb: 1fr6B
references: Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis.
references: Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase.
references: Role of residue Lys315 in the mechanism of action of the Enterobacter cloacae 908R beta-lactamase.
references: Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog.
references: The role of tyrosine 150 in catalysis of beta-lactam hydrolysis by AmpC beta-lactamase from Escherichia coli investigated by site-directed mutagenesis.
references: Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design.
references: Beta-secondary and solvent deuterium kinetic isotope effects on catalysis by the Streptomyces R61 DD-peptidase: comparisons with a structurally similar class C beta-lactamase.
references: Structure-function studies of Ser-289 in the class C beta-lactamase from Enterobacter cloacae P99.
references: Peptidase activity of beta-lactamases.
references: Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.
references: The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase.
references: Crystal structures of substrate and inhibitor complexes with ampc -lactamase: possible implications for substrate-assisted catalysis.
references: Expression, purification, crystallization and preliminary X-ray analysis of the native class C beta-lactamase from Enterobacter cloacae 908R and two mutants.
references: Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
references: Mechanism of reaction of acyl phosph(on)ates with the beta-lactamase of Enterobacter cloacae P99.
references: The relative catalytic efficiency of beta-lactamase catalyzed acyl and phosphyl transfer.
references: Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone.
references: Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site.
references: Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design.
references: Binding properties of a peptide derived from beta-lactamase inhibitory protein.
references: Mechanism of inhibition of the beta-lactamase of Enterobacter cloacae P99 by 1:1 complexes of vanadate with hydroxamic acids.
references: Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.
references: Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase.
references: Structural basis for imipenem inhibition of class C beta-lactamases.
references: Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.
references: pKa measurements from nuclear magnetic resonance of tyrosine-150 in class C beta-lactamase.
references: Role of beta-lactam carboxyl group on binding of penicillins and cephalosporins to class C beta-lactamases.
references: Structural aspects for evolution of beta-lactamases from penicillin-binding proteins.
references: Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
comment: This enzyme belongs to the class-C beta-lactamase family. Ser64 acts as a nucleophile, making a nucleophilic attack on beta-lactam ring, to form acyl-enzyme intermediate. According to the early studies ([1], [3], [4] & [5]), Tyr150 was considered to function as general acid-base. In contrast, the more recent report, [22], suggested substrate-assisted base. In this reported mechanism, C4' carboxylate of the substrate may activate Tyr150, which in turn may activate Ser64 by abstracting a proton from the serine residue during the acylation step [22]. Lys67 might play an intermediary role in transfer of the proton [22]. In the next deacylation step, a water molecule bound to Thr316 (and possibly Tyr150) makes an attack on the C8 carbonyl carbon of the acyl-enzyme intermediate, activating the Ser64 to be a leaving group [22]. The role of Tyr150 seems to be still controversial. However, considering the structure with ligand, Ser64, Tyr150, and Lys150 act as a nucleophile, acid-base, and a modulator for acid-base. Here, mainchain amide groups of Ser64 and Ser318 form an oxyanion hole. These suggest that the mechanism is very similar to that of trypsin (D00197).

Beta-lactamase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.710.10
catalytic domain: index.html

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

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

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

Penicillin
type: KeggSubstrate
references: KEGG:C00395
compound type: amide group
compound type: carboxyl group
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

1blsA
type: Pdb
references: 1bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

1blsB
type: Pdb
references: 1bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

1gceA
type: Pdb
references: 1gce
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gce
catalytic residue: SER 64;LYS 67;TYR 150;LYS 318;THR 319
main chain in catalysis: SER 64;SER 321

1c3bA
type: Pdb
references: 1c3b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3b
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1c3bB
type: Pdb
references: 1c3b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3b
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1fcmA
type: Pdb
references: 1fcm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fcm
catalytic residue: SER 61;LYS 64; ;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315
comment: mutant Q117L, Y147E

1fcmB
type: Pdb
references: 1fcm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fcm
catalytic residue: SER 61;LYS 64; ;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315
comment: mutant Q117L, Y147E

1fcnA
type: Pdb
references: 1fcn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fcn
catalytic residue: SER 61;LYS 64; ;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315
comment: mutant Q117L, Y147E

1fcnB
type: Pdb
references: 1fcn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fcn
catalytic residue: SER 61;LYS 64; ;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315
comment: mutant Q117L, Y147E

1fcoA
type: Pdb
references: 1fco
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fco
catalytic residue: SER 61;LYS 64;TYR 147;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315

1fcoB
type: Pdb
references: 1fco
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fco
catalytic residue: SER 61;LYS 64;TYR 147;LYS 312;THR 313
main chain in catalysis: SER 61;ALA 315

1fswA
type: Pdb
references: 1fsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fsw
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1fswB
type: Pdb
references: 1fsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fsw
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1fsyA
type: Pdb
references: 1fsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fsy
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1fsyB
type: Pdb
references: 1fsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fsy
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

2blsA
type: Pdb
references: 2bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

2blsB
type: Pdb
references: 2bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

2bltA
type: Pdb
references: 2blt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2blt
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

2bltB
type: Pdb
references: 2blt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2blt
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

3blsA
type: Pdb
references: 3bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

3blsB
type: Pdb
references: 3bls
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3bls
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;ALA 318

1fr1A
type: Pdb
references: 1fr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fr1
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

1fr1B
type: Pdb
references: 1fr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fr1
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

1fr6A
type: Pdb
references: 1fr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fr6
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

1fr6B
type: Pdb
references: 1fr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fr6
catalytic residue: SER 64;LYS 67;TYR 150;LYS 315;THR 316
main chain in catalysis: SER 64;SER 318

Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis.
type: BibliographicResource
comment: X-ray crystallography (2.0 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/2300174
journal: Nature
volume: 343
pages: 284-8
published year: 1990
authors:
  item: Oefner C
  item: D'Arcy A
  item: Daly JJ
  item: Gubernator K
  item: Charnas RL
  item: Heinze I
  item: Hubschwerlen C
  item: Winkler FK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase.
type: BibliographicResource
comment: X-ray crystallography (2 Angstroms)
medline id: 94068583
references: http://www.ncbi.nlm.nih.gov/pubmed/8248237
journal: Proc Natl Acad Sci U S A
volume: 90
pages: 11257-61
published year: 1993
authors:
  item: Lobkovsky E
  item: Moews PC
  item: Liu H
  item: Zhao H
  item: Frere JM
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05364

Role of residue Lys315 in the mechanism of action of the Enterobacter cloacae 908R beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8172894
journal: Biochemistry
volume: 33
pages: 5193-201
published year: 1994
authors:
  item: Monnaie D
  item: Dubus A
  item: Cooke D
  item: Marchand-Brynaert J
  item: Normark S
  item: Frere JM

Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog.
type: BibliographicResource
comment: X-ray crystallography (2.3 Angstroms)
medline id: 94263990
references: http://www.ncbi.nlm.nih.gov/pubmed/8204611
journal: Biochemistry
volume: 33
pages: 6762-72
published year: 1994
authors:
  item: Lobkovsky E
  item: Billings EM
  item: Moews PC
  item: Rahil J
  item: Pratt RF
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05364

The role of tyrosine 150 in catalysis of beta-lactam hydrolysis by AmpC beta-lactamase from Escherichia coli investigated by site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8031792
journal: Biochemistry
volume: 33
pages: 8577-86
published year: 1994
authors:
  item: Dubus A
  item: Normark S
  item: Kania M
  item: Page MG

Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design.
type: BibliographicResource
comment: X-ray crystallography (2.0-2.3 Angstroms)
medline id: 99036630
references: http://www.ncbi.nlm.nih.gov/pubmed/9819201
journal: Biochemistry
volume: 37
pages: 16082-92
published year: 1998
authors:
  item: Usher KC
  item: Blaszczak LC
  item: Weston GS
  item: Shoichet BK
  item: Remington SJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00811

Beta-secondary and solvent deuterium kinetic isotope effects on catalysis by the Streptomyces R61 DD-peptidase: comparisons with a structurally similar class C beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9931012
journal: Biochemistry
volume: 38
pages: 1469-77
published year: 1999
authors:
  item: Adediran SA
  item: Pratt RF

Structure-function studies of Ser-289 in the class C beta-lactamase from Enterobacter cloacae P99.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10049265
journal: Antimicrob Agents Chemother
volume: 43
pages: 543-8
published year: 1999
authors:
  item: Trepanier S
  item: Knox JR
  item: Clairoux N
  item: Sanschagrin F
  item: Levesque RC
  item: Huletsky A

Peptidase activity of beta-lactamases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10393100
journal: Biochem J
volume: 341
pages: 409-13
published year: 1999
authors:
  item: Rhazi N
  item: Galleni M
  item: Page MI
  item: Frere JM

Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.
type: BibliographicResource
comment: X-ray crystallography (1.8 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/10441119
journal: Biochemistry
volume: 38
pages: 10256-61
published year: 1999
authors:
  item: Crichlow GV
  item: Kuzin AP
  item: Nukaga M
  item: Mayama K
  item: Sawai T
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase.
type: BibliographicResource
comment: X-ray crystallography (2.25 Angstroms)
medline id: 20060984
references: http://www.ncbi.nlm.nih.gov/pubmed/10595535
journal: Protein Sci
volume: 8
pages: 2330-2337
published year: 1999
authors:
  item: Powers RA
  item: Blazquez J
  item: Weston GS
  item: Morosini MI
  item: Baquero F
  item: Shoichet BK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00811

Crystal structures of substrate and inhibitor complexes with ampc -lactamase: possible implications for substrate-assisted catalysis.
type: BibliographicResource
journal: J Am Chem Soc
volume: 122
pages: 10504-12
published year: 2000
authors:
  item: Patera A
  item: Blaszczak LC
  item: Shoichet BK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Expression, purification, crystallization and preliminary X-ray analysis of the native class C beta-lactamase from Enterobacter cloacae 908R and two mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11134945
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 162-4
published year: 2001
authors:
  item: Wouters J
  item: Charlier P
  item: Monnaie D
  item: Frere JM
  item: Fonze E

Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
type: BibliographicResource
comment: X-ray crystallography (1.75/1.90 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/11182316
journal: Chem Biol
volume: 8
pages: 17-31
published year: 2001
authors:
  item: Caselli E
  item: Powers RA
  item: Blasczcak LC
  item: Wu CY
  item: Prati F
  item: Shoichet BK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Mechanism of reaction of acyl phosph(on)ates with the beta-lactamase of Enterobacter cloacae P99.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11294628
journal: Biochemistry
volume: 40
pages: 4610-21
published year: 2001
authors:
  item: Kaur K
  item: Pratt RF

The relative catalytic efficiency of beta-lactamase catalyzed acyl and phosphyl transfer.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11300697
journal: Bioorg Chem
volume: 29
pages: 77-95
published year: 2001
authors:
  item: Slater MJ
  item: Laws AP
  item: Page MI

Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11371184
journal: Biochemistry
volume: 40
pages: 6233-9
published year: 2001
authors:
  item: Crichlow GV
  item: Nukaga M
  item: Doppalapudi VR
  item: Buynak JD
  item: Knox JR

Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11434768
journal: Biochemistry
volume: 40
pages: 7992-9
published year: 2001
authors:
  item: Trehan I
  item: Beadle BM
  item: Shoichet BK

Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11478888
journal: Biochemistry
volume: 40
pages: 9207-14
published year: 2001
authors:
  item: Powers RA
  item: Caselli E
  item: Focia PJ
  item: Prati F
  item: Shoichet BK

Binding properties of a peptide derived from beta-lactamase inhibitory protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11709298
journal: Antimicrob Agents Chemother
volume: 45
pages: 3279-86
published year: 2001
authors:
  item: Rudgers GW
  item: Huang W
  item: Palzkill T

Mechanism of inhibition of the beta-lactamase of Enterobacter cloacae P99 by 1:1 complexes of vanadate with hydroxamic acids.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11914079
journal: Biochemistry
volume: 41
pages: 4329-38
published year: 2002
authors:
  item: Bell JH
  item: Pratt RF

Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12005439
journal: Structure (Camb)
volume: 10
pages: 413-24
published year: 2002
authors:
  item: Beadle BM
  item: Trehan I
  item: Focia PJ
  item: Shoichet BK

Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12121656
journal: Structure (Camb)
volume: 10
pages: 1013-23
published year: 2002
authors:
  item: Powers RA
  item: Morandi F
  item: Shoichet BK

Structural basis for imipenem inhibition of class C beta-lactamases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12435704
journal: Antimicrob Agents Chemother
volume: 46
pages: 3978-80
published year: 2002
authors:
  item: Beadle BM
  item: Shoichet BK

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12482929
journal: Proc Natl Acad Sci U S A
volume: 99
pages: 16537-42
published year: 2002
authors:
  item: Baker K
  item: Bleczinski C
  item: Lin H
  item: Salazar-Jimenez G
  item: Sengupta D
  item: Krane S
  item: Cornish VW

pKa measurements from nuclear magnetic resonance of tyrosine-150 in class C beta-lactamase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12513696
journal: Biochem J
volume: 371
pages: 175-81
published year: 2003
authors:
  item: Kato-Toma Y
  item: Iwashita T
  item: Masuda K
  item: Oyama Y
  item: Ishiguro M

Role of beta-lactam carboxyl group on binding of penicillins and cephalosporins to class C beta-lactamases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12696055
journal: Proteins
volume: 51
pages: 442-52
published year: 2003
authors:
  item: Fenollar-Ferrer C
  item: Frau J
  item: Donoso J
  item: Munoz F

Structural aspects for evolution of beta-lactamases from penicillin-binding proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12904027
journal: J Am Chem Soc
volume: 125
pages: 9612-8
published year: 2003
authors:
  item: Meroueh SO
  item: Minasov G
  item: Lee W
  item: Shoichet BK
  item: Mobashery S

Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14521155
journal: Cell Mol Life Sci
volume: 60
pages: 1764-73
published year: 2003
authors:
  item: Wouters J
  item: Fonze E
  item: Vermeire M
  item: Frere JM
  item: Charlier P

beta-lactamase A, B, C
type: KeggEnzyme

beta-lactamase AME I
type: KeggEnzyme

cephalosporin-beta-lactamase
type: KeggEnzyme

TransitionStateAnalogue
pdb: 1blsA
ligand het code: IPP

TransitionStateAnalogue
pdb: 1blsB
ligand het code: IPP

TransitionStateAnalogue
pdb: 1c3bA
ligand het code: BZB

TransitionStateAnalogue
pdb: 1c3bB
ligand het code: BZB

IntermediateAnalogue
pdb: 1fcmA
ligand het code: CXN

IntermediateAnalogue
pdb: 1fcmB
ligand het code: CXN

IntermediateAnalogue
pdb: 1fcnA
ligand het code: LOR

IntermediateAnalogue
pdb: 1fcnB
ligand het code: LOR

IntermediateAnalogue
pdb: 1fcoA
ligand het code: MOX

IntermediateAnalogue
pdb: 1fcoB
ligand het code: MOX

TransitionStateAnalogue
pdb: 1fswA
ligand het code: CTB

TransitionStateAnalogue
pdb: 1fswB
ligand het code: CTB

TransitionStateAnalogue
pdb: 1fsyA
ligand het code: 105

TransitionStateAnalogue
pdb: 1fsyB
ligand het code: 105

TransitionStateAnalogue
pdb: 3blsA
ligand het code: APB

TransitionStateAnalogue
pdb: 3blsB
ligand het code: APB

IntermediateAnalogue
pdb: 1fr6A
ligand het code: AZR

IntermediateAnalogue
pdb: 1fr6B
ligand het code: AZR

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.3
reference step: 3

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.11261

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.6767-6771

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.7, p.8584-8586
reference step: 2

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.2334-2336

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.1, p.10511-10512

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.2
reference step: 2

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.4619-4620

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.6238-6239

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig.1(A), Fig.5, p.418-419, p.421
reference step: 2

ReferenceForCatalyticMechanism
reference index: 26
reference section: p.180

ReferenceForCatalyticMechanism
reference index: 29
reference section: p.1768-1769