Inactivation of Bacillus cereus beta-lactamase I by 6 beta-bromopencillanic acid: mechanism.
about
Identification of the site of covalent attachment of nafcillin, a reversible suicide inhibitor of beta-lactamaseActive-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus GStructural Basis of the Inhibition of Class A β-Lactamases and Penicillin-Binding Proteins by 6-β-IodopenicillanateInactivation of the thiol RTEM-1 beta-lactamase by 6-beta-bromopenicillanic acid. Identity of the primary active-site nucleophile6-beta-Iodopenicillanate as a probe for the classification of beta-lactamasesThe K1 beta-lactamase of Klebsiella pneumoniaeInteraction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39Thiol-beta-lactamase: replacement of the active-site serine of RTEM beta-lactamase by a cysteine residue.beta-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptorsOligonucleotide-directed mutagenesis as a general and powerful method for studies of protein function.Site-directed mutagenesis of beta-lactamase I: role of Glu-166.Active-site serine mutants of the Streptomyces albus G beta-lactamase.Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.The potential use of mechanism-based enzyme inactivators in medicine.Beta-lactamases: molecular studies.Plasmid-determined resistance to antimicrobial drugs and toxic metal ions in bacteria.Antibiotic resistance in pathogenic and producing bacteria, with special reference to beta-lactam antibiotics.Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus.The inhibition of class C beta-lactamases by boronic acids.Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.Interactions between active-site-serine beta-lactamases and mechanism-based inactivators: a kinetic study and an overview.Unexpected influence of ionic strength on branched-pathway interactions between beta-lactamases and beta-halogenopenicillanates.The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.Trapping the acyl-enzyme intermediate in beta-lactamase I catalysis.Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases.The active site of the P99 beta-lactamase from Enterobacter cloacae.Active sites of beta-lactamases. The chromosomal beta-lactamases of Pseudomonas aeruginosa and Escherichia coli.Amino acid sequence homologies between Escherichia coli penicillin-binding protein 5 and class a β-lactamases
P2860
Q24527332-83E778AC-F1F1-4DD3-966F-BAA88368F086Q24529946-920F9E20-AAFD-4320-A2B7-8896609EA3F8Q27658217-FA057845-3C19-4C7D-B081-0D9B424F2F67Q28359796-15BC3D76-4555-4DFE-A794-97F5DF67D10CQ28360533-52CF624E-F270-4A68-B555-5666D08DD692Q28361337-43D5F296-B045-466D-A6D1-35CEC1CDE828Q28366211-45F0C552-7142-40DA-AA63-868E43CF6AE3Q34270726-BEDBD1C5-AE29-443F-A23A-05F254C3A4E5Q36250771-C8054716-749E-4AFC-AFC7-D2467211B4FCQ36317552-1A8CD972-1167-4208-ABA1-FB6AB482877AQ38308727-2765996C-2049-4A88-B9A6-1DE8F3EF2C18Q38334034-7815EB84-669B-4300-BB34-827FD1A193B4Q38338744-556CFCE2-7CDF-4B47-BEDE-84F381E535A3Q38348221-541DE6C8-95FB-4955-B91F-BA9D3271F023Q39568018-F96B27F6-514C-4FB3-AD10-DFC87548A2C7Q39840462-3533A3A1-91B2-422D-8990-B95F171F158DQ40161230-0B2578BB-ED52-4C49-BC3A-889E8DC002F3Q40270998-A5ADEEC8-D11B-47B7-828A-C5A5225EFE8DQ41866402-501336CC-6511-4ACB-B400-103B276ED0E8Q41876580-B8E8414D-258F-47AF-AFE3-F5517865AA07Q41940976-5A8C162B-645B-427D-AB16-A65A55D05ACCQ41968772-6648ED78-2144-4C66-971E-96DAE47C6423Q42123217-FE274FBA-14B1-462B-850C-7FB4251D0202Q42130830-25537547-B25F-4C16-BC31-976C04623E6EQ42804291-92A27651-8794-45ED-B815-4D729FB52450Q42817920-A19DBE21-45A3-4526-BE8D-12A215D357E8Q42820512-8970CF8E-990D-4A60-B3BE-F25B3FB7177AQ42848209-CAC3AA47-1E33-4945-995F-3C9684098172Q46601814-C969ECB6-A628-476B-9ECE-D2DDE6BACD5CQ58483907-7D3AC24C-E9A5-4B19-8281-4B06897CB494
P2860
Inactivation of Bacillus cereus beta-lactamase I by 6 beta-bromopencillanic acid: mechanism.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@en
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@nl
type
label
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@en
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@nl
prefLabel
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@en
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@nl
P356
P1433
P1476
Inactivation of Bacillus cereu ...... mopencillanic acid: mechanism.
@en
P2093
P304
P356
10.1021/BI00558A017
P407
P577
1980-08-01T00:00:00Z