Apramycin Biosynthesis: Structure and Mechanism of Action of a New-Type Transaldolase AprG from <i>Streptoalloteichus tenebrarius</i>

A distinct transaldolase (TAL) termed AprG accounts for the biosynthesis of the octose core of apramycin. AprG transfers a two-carbon unit of a donor substrate such as GalNAc or GlcNAc to the acceptor substrate 6′-oxolividamine, followed by intramolecular cyclization to generate the bicyclic product...

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Auteur principal:	Zhenzhen Xie (12610822) (author)
Autres auteurs:	Lilan Zhang (1308402) (author), Qiru Li (22188233) (author), Jian-Wen Huang (3208149) (author), Yanting He (2426158) (author), Hualin Zhang (11948553) (author), Xinyue Wang (286629) (author), Jian Min (1965868) (author), Chun-Chi Chen (103097) (author), Rey-Ting Guo (449264) (author)
Publié:	2025
Sujets:	Biophysics Biochemistry Computational Biology Biological Sciences not elsewhere classified β )< sub streptoalloteichus tenebrarius </ mutagenesis experiments imply termed aprg accounts molecular mechanism underlying α )< sub represent different stages oh interaction networks base intermediates formed also proposed accordingly type transaldolase aprg putative acceptor substrate aprg toward galnac catalytic reaction mechanism interaction networks catalytic reaction base intermediates acceptor substrate distinct transaldolase aprg transfers donor substrate octose core might contribute key residue intramolecular cyclization including galnac donor substrates directly engages crystal structures catalyzed process carbon unit canonical tals binding site binding pose bicyclic product angular strain
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Apramycin Biosynthesis: Structure and Mechanism of Action of a New-Type Transaldolase AprG from <i>Streptoalloteichus tenebrarius</i>

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