Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks

Journal of Inorganic Biochemistry

Volumn 162, Issue , 2016, Pages 366-375

  Miraula, Manfredi ^a,b   Schenk, Gerhard ^b   Mitić, Nataša ^a  

^a NATIONAL UNIVERSITY OF IRELAND   (Ireland)

^b UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Antibiotic resistance; Binuclear metallohydrolases; Functional promiscuity; Metallo beta lactamases; Quorum sensing

Indexed keywords

ANTIBIOTIC AGENT; CALCIUM; COBALT; COPPER; GLUCONOLACTONASE; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTOYLGLUTATHIONE LYASE; METALLO BETA LACTAMASE; METALLO BETA LACTAMASE MIM 1; METALLO BETA LACTAMASE MIM 2; N ACYLHOMOSERINE LACTONE; UNCLASSIFIED DRUG; ZINC; BACTERIAL PROTEIN; BETA LACTAMASE; CARBOXYLESTERASE; GLUTATHIONE; MANGANESE; N-ACYL HOMOSERINE LACTONASE; RECOMBINANT PROTEIN; S-LACTOYLGLUTATHIONE; THIOL ESTER HYDROLASE;

ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; CHEMICAL COMPOSITION; COMPARATIVE STUDY; ENZYME ACTIVITY; MARINE BACTERIUM; MOLECULAR DOCKING; NOVOSPHINGOBIUM PENTAROMATIVORANS; PHYLOGENY; QUORUM SENSING; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SIMIDUIA AGARIVORANS; STRUCTURAL HOMOLOGY; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; PROTEIN SECONDARY STRUCTURE; PSEUDOMONADACEAE; SEQUENCE HOMOLOGY; SPHINGOMONADACEAE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BETA-LACTAMASES; CALCIUM; CARBOXYLIC ESTER HYDROLASES; CLONING, MOLECULAR; COBALT; COPPER; ESCHERICHIA COLI; GENE EXPRESSION; GLUTATHIONE; KINETICS; MANGANESE; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONADACEAE; QUORUM SENSING; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPHINGOMONADACEAE; SUBSTRATE SPECIFICITY; THIOLESTER HYDROLASES; ZINC;

EID: 84953208647     PISSN: 01620134     EISSN: 18733344     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2015.12.014     Document Type: Article

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