Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.
Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
D Cole
DC
Stevens
Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Drew T
DT
Wagner
Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Hannah R
HR
Manion
Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Bradley K
BK
Alexander
Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.|Department of Chemistry, The University of Texas at Austin, Austin, Texas, USA.
Adrian T
AT
Keatinge-Clay
D000069977:Bacillus amyloliquefaciens / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D003543:Cysteamine / Q000031:analogs & derivatives* / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D007700:Kinetics; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism*; D048630:Polyketide Synthases / Q000235:genetics / Q000378:metabolism*; D011551:Pseudomonas fluorescens / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
D011994:Recombinant Proteins; D003543:Cysteamine; D048630:Polyketide Synthases; D008780:Methyltransferases