Histidine residues of zinc ligands in beta-lactamase II.
about
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein foldStructural effects of the active site mutation cysteine to serine inBacillus cereuszinc-β-lactamaseThe exchange of histidine C-2 protons in superoxide dismutases. A novel method for assigning histidine-metal ligands in proteins.Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli.Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism.Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance.Penicillinase active sites: labelling of serine-44 in beta-lactamase I by 6beta-bromopenicillanic acid.Antibiotic resistance in pathogenic and producing bacteria, with special reference to beta-lactam antibiotics.Biochemical properties of inducible beta-lactamases produced from Xanthomonas maltophilia.Identification of histidine residues that act as zinc ligands in beta-lactamase II by differential tritium exchange.The 1H nuclear-magnetic-resonance spectroscopy of cobalt(II)-beta-lactamase II.The pH-dependence of class B and class C beta-lactamases.Production of a variant of beta-lactamase II with selectively decreased cephalosporinase activity by a mutant of Bacillus cereus 569/H/9.An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35 nm resolution.Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase.The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy.A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate.The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase.Biomimetic hydrolysis of penicillin G catalyzed by dinuclear zinc(II) complexes: structure-activity correlations in beta-lactamase model systems.
P2860
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P2860
Histidine residues of zinc ligands in beta-lactamase II.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
Histidine residues of zinc ligands in beta-lactamase II.
@en
Histidine residues of zinc ligands in beta-lactamase II.
@nl
type
label
Histidine residues of zinc ligands in beta-lactamase II.
@en
Histidine residues of zinc ligands in beta-lactamase II.
@nl
prefLabel
Histidine residues of zinc ligands in beta-lactamase II.
@en
Histidine residues of zinc ligands in beta-lactamase II.
@nl
P2093
P2860
P356
P1433
P1476
Histidine residues of zinc ligands in beta-lactamase II.
@en
P2093
P2860
P304
P356
10.1042/BJ1750441
P407
P577
1978-11-01T00:00:00Z