Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis. Academic Article

abstract

• 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.

authors

• Begley, Tadhg

published proceedings

• Bioorg Chem

altmetric score

• 3

author list (cited authors)

• Jenkins, A. L., Zhang, Y., Ealick, S. E., & Begley, T. P.

citation count

• 15

complete list of authors

• Jenkins, Amy L||Zhang, Yang||Ealick, Steven E||Begley, Tadhg P

publication date

• January 1, 2008 11:11 AM

publisher

• Elsevier  Publisher
• Elsevier BV  Publisher

published in

• Bioorganic Chemistry  Journal

keywords

• Bacillus Subtilis
• Binding Sites
• Catalysis
• Hydrolases
• Hydrolysis
• Models, Molecular
• Molecular Structure
• Mutagenesis, Site-Directed
• Structure-Activity Relationship
• Thiamine

PubMed Central ID

• 18054064

Digital Object Identifier (DOI)

• 10.1016/j.bioorg.2007.10.005

start page

• 29

end page

• 32

volume

• 36

issue

• 1