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beta-Lactamase
Known as:
Beta lactamase
, beta-Lactamases [Chemical/Ingredient]
, Beta lactamases
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Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these…
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National Institutes of Health
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Related topics
Related topics
50 relations
Broader (1)
Amidohydrolases
Narrower (44)
AmpC beta-lactamases
CMY-10 beta-lactamase
CTX-M-27, E coli
CTX-M-4 protein, Salmonella typhimurium
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Beta Lactamase Screening Method
Beta lactamase.extended spectrum:Susc:Pt:Isolate:OrdQn
In Blood
Process of secretion
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
1985
1985
Formadicins, new monocyclic beta-lactam antibiotics of bacterial origin. I. Taxonomy, fermentation and biological activities.
N. Katayama
,
Yukimasa Nozaki
,
Kenji Okonogi
,
H. Ono
,
Setsuo Harada
,
H. Okazaki
Journal of antibiotics (Tokyo. )
1985
Corpus ID: 22570654
A Gram-negative bacterium produces new monocyclic beta-lactam antibiotics with a formylamino substituent, named formadicins A, B…
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1984
1984
Penicillanic acid sulfone: nature of irreversible inactivation of RTEM beta-lactamase from Escherichia coli.
D. Brenner
,
Jeremy R. Knowles
Biochemistry
1984
Corpus ID: 42387752
When penicillanic acid sulfone in large molar excess is incubated with the RTEM beta-lactamase, the enzyme becomes inactivated…
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1984
1984
6-(Methoxymethylene)penicillanic acid: inactivator of RTEM beta-lactamase from Escherichia coli.
D. Brenner
,
Jeremy R. Knowles
Biochemistry
1984
Corpus ID: 21038604
The Z and E isomers of 6-(methoxymethylene)-penicillanic acid have been synthesized, and their interaction with the RTEM beta…
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Highly Cited
1981
Highly Cited
1981
Inactivation of the RTEM beta-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme.
J. Fisher
,
Robert L. Charnas
,
Scott M. Bradley
,
Jeremy R. Knowles
Biochemistry
1981
Corpus ID: 43894138
The characteristics of the reaction of a number of mechanism-based inactivators of the RTEM beta-lactamase have suggested that a…
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1981
1981
A set of bacterial strains for evaluation of beta-lactamase-stability of beta-lactam antibiotics.
T. Sawai
,
Takashi Yoshida
,
Kikuo Tsukamoto
,
S. Yamagishi
Journal of antibiotics (Tokyo. )
1981
Corpus ID: 26710361
A set of bacterial strains composed of nine bacterial groups, with each made up of three or four strains, was used to estimate…
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1979
1979
The comparative beta-lactamase resistance and inhibitory activity of 1-oxa cephalosporin, cefoxitin and cefotaxime.
Kwung P. Fu
,
H. Neu
Journal of antibiotics (Tokyo. )
1979
Corpus ID: 27319024
The beta-lactamase stability and inhibitory activity of 1-oxa cephalosporin, (6R,7R)-7-[[carboxy(4-hydroxyphenyl)acetyl]amino]-7…
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1979
1979
Penetration through the gram-negative cell wall: a co-determinant of the efficacy of beta-lactam antibiotics.
W. Zimmermann
International journal of clinical pharmacology…
1979
Corpus ID: 27740728
Resistance of gram-negative bacteria to beta-lactam antibiotics is based mainly on two mechanisms: hydrolysis by beta-lactamases…
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Highly Cited
1978
Highly Cited
1978
A sulfone beta-lactam compound which acts as a beta-lactamase inhibitor.
Nalinee Aswapokee
,
H. Neu
Journal of antibiotics (Tokyo. )
1978
Corpus ID: 24425865
CP-45,899 [3,3-dimethyl-7-oxo-4-thia-1-azabicyclo(3,2,0)heptane-2-carboxylic acid, 4,4-dioxide [2S-(2alpha,5alpha)]] has low…
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1978
1978
Histidine residues of zinc ligands in beta-lactamase II.
G. Baldwin
,
Alphonse Galdes
,
H. Hill
,
B. E. Smith
,
S. G. Waley
,
E. Abraham
Biochemical Journal
1978
Corpus ID: 43072402
1. The Zn(II)-requiring beta-lactamase from Bacillus cereus 569/H/9, which has two zinc-binding sites, was examined by 270 MHz 1H…
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1976
1976
Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the phospholipopeptide region.
S. Yamamoto
,
J. Lampen
Proceedings of the National Academy of Sciences…
1976
Corpus ID: 20185945
The membrane penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) of Bacillus licheniforis 749/C, which appears to…
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