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Beta-lactamase database (BLDB) - structure and function

Beta-lactamase database (BLDB) - structure and function

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2195228368

Beta-lactamase database (BLDB) - structure and function

About this item

Full title

Beta-lactamase database (BLDB) - structure and function

Publisher

England: Taylor & Francis

Journal title

Journal of enzyme inhibition and medicinal chemistry, 2017-01, Vol.32 (1), p.917-919

Language

English

Formats

Publication information

Publisher

England: Taylor & Francis

More information

Scope and Contents

Contents

Beta-Lactamase Database (BLDB) is a comprehensive, manually curated public resource providing up-to-date structural and functional information focused on this superfamily of enzymes with a great impact on antibiotic resistance. All the enzymes reported and characterised in the literature are presented according to the class (A, B, C and D), family and subfamily to which they belong. All three-dimensional structures of β-lactamases present in the Protein Data Bank are also shown. The characterisation of representative mutants and hydrolytic profiles (kinetics) completes the picture and altogether these four elements constitute the essential foundation for a better understanding of the structure-function relationship within this enzymes family. BLDB can be queried using different protein- and nucleotide-based BLAST searches, which represents a key feature of particular importance in the context of the surveillance of the evolution of the antibiotic resistance. BLDB is available online at
http://bldb.eu
without any registration and supports all modern browsers....

Alternative Titles

Full title

Beta-lactamase database (BLDB) - structure and function

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2195228368

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2195228368

Other Identifiers

ISSN

1475-6366,1475-6374

E-ISSN

1475-6374

DOI

10.1080/14756366.2017.1344235

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