Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.
TenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described.
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Amy L
AL
Jenkins
Yang
Y
Zhang
Steven E
SE
Ealick
Tadhg P
TP
Begley
D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D002384:Catalysis; D006867:Hydrolases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D006868:Hydrolysis; D008958:Models, Molecular; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D013329:Structure-Activity Relationship; D013831:Thiamine / Q000737:chemistry / Q000378:metabolism*
D006867:Hydrolases; C022731:thiaminase II; D013831:Thiamine