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Volumn 8, Issue 8, 2001, Pages 684-689
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Structure of β-lactam synthetase reveals how to synthesize antibiotics instead of asparagine
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINE PHOSPHATE;
ADENOSINE TRIPHOSPHATE;
ADENOSINE TRIPHOSPHATE DERIVATIVE;
ANTIBIOTIC AGENT;
ASPARAGINE;
ASPARTIC ACID;
BETA LACTAM ANTIBIOTIC;
BETA LACTAM SYNTHETASE;
BETA LACTAMASE INHIBITOR;
CLAVULANIC ACID;
FERROUS ION;
ISOPENICILLIN N SYNTHETASE;
MAGNESIUM ION;
OXYGEN;
PENICILLINASE;
SYNTHETASE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
ARTICLE;
CATALYSIS;
CRYSTAL STRUCTURE;
DRUG SYNTHESIS;
ENZYME INHIBITION;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
EVOLUTION;
GENETIC PROCEDURES;
OPTICAL RESOLUTION;
PRIORITY JOURNAL;
SEQUENCE ANALYSIS;
SEQUENCE HOMOLOGY;
STREPTOMYCES CLAVULIGERUS;
ADENOSINE TRIPHOSPHATE;
AMIDOHYDROLASES;
AMINO ACID SEQUENCE;
ANTI-BACTERIAL AGENTS;
ASPARAGINE;
ASPARTATE-AMMONIA LIGASE;
BINDING SITES;
CLAVULANIC ACID;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
EVOLUTION, MOLECULAR;
MAGNESIUM;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE ALIGNMENT;
STREPTOMYCES;
STRUCTURE-ACTIVITY RELATIONSHIP;
ESCHERICHIA COLI;
STREPTOMYCES CLAVULIGERUS;
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EID: 0034885889
PISSN: 10728368
EISSN: None
Source Type: Journal
DOI: 10.1038/90394 Document Type: Article |
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Times cited : (60)
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References (34)
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