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Inside Cover: The A9 Core Sequence from NRPS Adenylation Domain Is Relevant for Thioester Formation (ChemBioChem 13/2012)
Author(s) -
BučevićPopović Viljemka,
Šprung Matilda,
Soldo Barbara,
PavelaVrančič Maja
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201290054
Subject(s) - adenylylation , domain (mathematical analysis) , sequence (biology) , cover (algebra) , mutagenesis , chemistry , stereochemistry , substrate (aquarium) , peptide sequence , combinatorial chemistry , biology , biochemistry , biosynthesis , enzyme , mutation , gene , engineering , ecology , mechanical engineering , mathematical analysis , mathematics
The inside cover picture shows the conserved A9 core sequence in the NRPS adenylation (A) domain. Mutagenesis study on a domain from the tyrocidine biosynthetic system reveals that the sequence is important for the transfer of activated amino acid substrate to the partner thiolation (T) domain. For further details see the paper by V. Bučević‐Popović, M. Pavela‐Vrančič et al. on p. 1913;ff.