Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substra...
Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases
About this item
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Publisher
Berlin/Heidelberg: Springer Berlin Heidelberg
Journal title
Language
English
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Publisher
Berlin/Heidelberg: Springer Berlin Heidelberg
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Scope and Contents
Contents
Understanding the metabolic potential of organisms or a bacterial community based on their (meta) genome requires the reliable prediction of an enzyme’s function from its amino acid sequence. Besides a remarkable development in prediction algorithms, the substrate scope of sequences with low identity to well-characterized enzymes remains often very...
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Full title
Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases
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Record Identifier
TN_cdi_swepub_primary_oai_DiVA_org_kth_180823
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_kth_180823
Other Identifiers
ISSN
0175-7598,1432-0614
E-ISSN
1432-0614
DOI
10.1007/s00253-015-7275-9
