Literature DB >> 4957174

Zinc as a cofactor for cephalosporinase from Bacillus cereus 569.

L D Sabath, E P Abraham.   

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Year:  1966        PMID: 4957174      PMCID: PMC1264844          DOI: 10.1042/bj0980011c

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


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  5 in total

1.  Metallocarboxypeptidasesubstrate complexes.

Authors:  J E COLEMAN; B L VALLEE
Journal:  Biochemistry       Date:  1962-11       Impact factor: 3.162

2.  Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicillanic acidas substrates, inhibitors and inducers of penicillinases.

Authors:  B CROMPTON; M JAGO; K CRAWFORD; G G NEWTON; E P ABRAHAM
Journal:  Biochem J       Date:  1962-04       Impact factor: 3.857

3.  A comparison of the action of penicillinase on benzylpenicillin and cephalosporin N and the competitive inhibition of penicillinase by cephalosporin C.

Authors:  E P ABRAHAM; G G NEWTON
Journal:  Biochem J       Date:  1956-08       Impact factor: 3.857

4.  Penicillinase adaptation in Bacillus cereus; an analysis of three phases in the response of logarithmically growing cultures to induction of penicillinase formation by penicillin.

Authors:  M R POLLOCK
Journal:  Br J Exp Pathol       Date:  1952-12

5.  Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea.

Authors:  L D Sabath; M Jago; E P Abraham
Journal:  Biochem J       Date:  1965-09       Impact factor: 3.857

  5 in total
  32 in total

1.  Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase.

Authors:  James J A Huntley; Walter Fast; Stephen J Benkovic; Peter E Wright; H Jane Dyson
Journal:  Protein Sci       Date:  2003-07       Impact factor: 6.725

2.  Independent origins of subgroup Bl + B2 and subgroup B3 metallo-beta-lactamases.

Authors:  Barry G Hall; Stephen J Salipante; Miriam Barlow
Journal:  J Mol Evol       Date:  2004-07       Impact factor: 2.395

3.  Folding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1.

Authors:  Zhenxin Hu; Gopal R Periyannan; Michael W Crowder
Journal:  Anal Biochem       Date:  2008-04-07       Impact factor: 3.365

4.  A structural view of the antibiotic degradation enzyme NDM-1 from a superbug.

Authors:  Yu Guo; Jing Wang; Guojun Niu; Wenqing Shui; Yuna Sun; Honggang Zhou; Yaozhou Zhang; Cheng Yang; Zhiyong Lou; Zihe Rao
Journal:  Protein Cell       Date:  2011-06-02       Impact factor: 14.870

Review 5.  Overcoming differences: The catalytic mechanism of metallo-β-lactamases.

Authors:  María-Rocío Meini; Leticia I Llarrull; Alejandro J Vila
Journal:  FEBS Lett       Date:  2015-08-20       Impact factor: 4.124

Review 6.  Past and Present Perspectives on β-Lactamases.

Authors:  Karen Bush
Journal:  Antimicrob Agents Chemother       Date:  2018-09-24       Impact factor: 5.191

7.  The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.

Authors:  Caroline Montagner; Michaël Nigen; Olivier Jacquin; Nicolas Willet; Mireille Dumoulin; Andreas Ioannis Karsisiotis; Gordon C K Roberts; Christian Damblon; Christina Redfield; André Matagne
Journal:  J Biol Chem       Date:  2016-05-27       Impact factor: 5.157

8.  Investigation of Dipicolinic Acid Isosteres for the Inhibition of Metallo-β-Lactamases.

Authors:  Allie Y Chen; Pei W Thomas; Zishuo Cheng; Nasa Y Xu; David L Tierney; Michael W Crowder; Walter Fast; Seth M Cohen
Journal:  ChemMedChem       Date:  2019-05-24       Impact factor: 3.466

9.  Penicillinases of Klebsiella pneumoniae and their phylogenetic relationship to penicillinases mediated by R factors.

Authors:  T Sawai; S Yamagishi; S Mitsuhashi
Journal:  J Bacteriol       Date:  1973-09       Impact factor: 3.490

10.  Evaluation of a new Etest for detecting metallo-beta-lactamases in routine clinical testing.

Authors:  Timothy R Walsh; Anne Bolmström; Anette Qwärnström; Ana Gales
Journal:  J Clin Microbiol       Date:  2002-08       Impact factor: 5.948

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